Reference - PMID:30715423 - Queuine links translational control in eukaryotes to a micronutrient from bacteria.
Reference summary
- PubMed ID
- PMID:30715423
- Title
- Queuine links translational control in eukaryotes to a micronutrient from bacteria.
- Authors
- Müller M, Legrand C, Tuorto F, Kelly VP, Atlasi Y, Lyko F, Ehrenhofer-Murray AE
- Citation
- Nucleic Acids Res 2019 Apr 23;47(7):3711-3727
- Publication year
- 2019
- Abstract
- In eukaryotes, the wobble position of tRNA with a GUN anticodon is modified to the 7-deaza-guanosine derivative queuosine (Q34), but the original source of Q is bacterial, since Q is synthesized by eubacteria and salvaged by eukaryotes for incorporation into tRNA. Q34 modification stimulates Dnmt2/Pmt1-dependent C38 methylation (m5C38) in the tRNAAsp anticodon loop in Schizosaccharomyces pombe. Here, we show by ribosome profiling in S. pombe that Q modification enhances the translational speed of the C-ending codons for aspartate (GAC) and histidine (CAC) and reduces that of U-ending codons for asparagine (AAU) and tyrosine (UAU), thus equilibrating the genome-wide translation of synonymous Q codons. Furthermore, Q prevents translation errors by suppressing second-position misreading of the glycine codon GGC, but not of wobble misreading. The absence of Q causes reduced translation of mRNAs involved in mitochondrial functions, and accordingly, lack of Q modification causes a mitochondrial defect in S. pombe. We also show that Q-dependent stimulation of Dnmt2 is conserved in mice. Our findings reveal a direct mechanism for the regulation of translational speed and fidelity in eukaryotes by a nutrient originating from bacteria.
