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Reference - PMID:18794354 - Schizosaccharomyces pombe Ddb1 recruits substrate-specific adaptor proteins through a novel protein motif, the DDB-box.

Reference summary

PubMed ID
PMID:18794354
Title
Schizosaccharomyces pombe Ddb1 recruits substrate-specific adaptor proteins through a novel protein motif, the DDB-box.
Authors
Fukumoto Y, Dohmae N, Hanaoka F
Citation
Mol Cell Biol 2008 Nov;28(22):6746-56
Publication year
2008
Abstract
DDB1 was isolated as a UV-damaged DNA-binding protein, but recent studies established that it plays a role as a component of cullin 4A ubiquitin ligases. Cullin-RING complexes are the largest known ubiquitin ligase family, with hundreds of substrate-specific adaptor subunits and which are defined by characteristic motifs. A common motif for DDB1/cullin 4 ubiquitin ligases, a WDXR motif, was recently reported. Here, we show that Schizosaccharomyces pombe Ddb1 associates with several WD40 repeat proteins that share a novel protein motif designated the DDB-box, a motif essential for interaction with Ddb1 and independent of WD40 repeats, unlike the WDXR motif. We also show that ddb1(+) and the putative CSA homolog ckn1(+) are involved in transcription-coupled nucleotide excision repair and that the DDB-box is essential for the ckn1(+) function in vivo. These data indicate that the DDB-box is another common motif which defines adaptor proteins for DDB1/cullin 4 ubiquitin ligases.

Annotation

GO biological process

GO:0006283 - transcription-coupled nucleotide-excision repair

Genes:

GO cellular component

GO:0070912 - Ddb1-Ckn1 complex

Genes:

GO:0070913 - Ddb1-Wdr21 complex

Genes:

Modification

MOD:01148 - ubiquitinylated lysine

Genes:

Protein sequence feature

SO:0001804 - DDB_box

Genes:

Orthologs