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Queuine links translational control in eukaryotes to a micronutrient from bacteria

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/P...

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Main Authors: Müller, Martin (Author) , Legrand, Carine (Author) , Tuorto, Francesca (Author) , Kelly, Vincent P. (Author) , Atlasi, Yaser (Author) , Lyko, Frank (Author) , Ehrenhofer-Murray, Ann Elizabeth (Author)
Format: Article (Journal)
Language:English
Published: 23 April 2019
In: Nucleic acids research
Year: 2019, Volume: 47, Issue: 7, Pages: 3711-3727
ISSN:1362-4962
DOI:10.1093/nar/gkz063
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1093/nar/gkz063
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Author Notes:Martin Müller, Carine Legrand, Francesca Tuorto, Vincent P. Kelly, Yaser Atlasi, Frank Lyko and Ann E. Ehrenhofer-Murray
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Summary: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.
Item Description:Veröffentlicht am 1. Februar 2019
Gesehen am 17.01.2022
Physical Description:Online Resource
ISSN:1362-4962
DOI:10.1093/nar/gkz063

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