Queuine links translational control in eukaryotes to a micronutrient from bacteria

• Verfasst von: Müller, Martin [VerfasserIn]
• Verfasst von: Legrand, Carine [VerfasserIn]
• Verfasst von: Tuorto, Francesca [VerfasserIn]
• Verfasst von: Kelly, Vincent P. [VerfasserIn]
• Verfasst von: Atlasi, Yaser [VerfasserIn]
• Verfasst von: Lyko, Frank [VerfasserIn]
• Verfasst von: Ehrenhofer-Murray, Ann Elizabeth [VerfasserIn]
• Titel: Queuine links translational control in eukaryotes to a micronutrient from bacteria
• Verf.angabe: Martin Müller, Carine Legrand, Francesca Tuorto, Vincent P. Kelly, Yaser Atlasi, Frank Lyko and Ann E. Ehrenhofer-Murray
• E-Jahr: 2019
• Jahr: 23 April 2019
• Umfang: 17 S.
• Fussnoten: Veröffentlicht am 1. Februar 2019 ; Gesehen am 17.01.2022
• Titel Quelle: Enthalten in: Nucleic acids research
• Ort Quelle: Oxford : Oxford Univ. Press, 1974
• Jahr Quelle: 2019
• Band/Heft Quelle: 47(2019), 7, Seite 3711-3727
• ISSN Quelle: 1362-4962
• DOI: doi:10.1093/nar/gkz063
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1786288419

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.