Journal
MOLECULAR CELL
Volume 53, Issue 4, Pages 645-654Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2013.12.028
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Funding
- University of Oxford Clarendon Award
- Russian Foundation for Basic Research [11-04-00840, 12-04-00147, 12-04-33085]
- Russian Academy of Sciences
- Marie Curie IEF Fellowship [298603]
- Wellcome Trust
- Ludwig Institute for Cancer Research
- BBSRC
- OAK foundation
- MRC New Investigator Award
- BBSRC [BB/L004275/1] Funding Source: UKRI
- MRC [MR/K010816/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/L004275/1] Funding Source: researchfish
- Medical Research Council [MR/K010816/1] Funding Source: researchfish
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Efficient stop codon recognition and peptidyl-tRNA hydrolysis are essential in order to terminate translational elongation and maintain protein sequence fidelity. Eukaryotic translational termination is mediated by a release factor complex that includes eukaryotic release factor 1 (eRF1) and eRF3. The N terminus of eRF1 contains highly conserved sequence motifs that couple stop codon recognition at the ribosomal A site to peptidyl-tRNA hydrolysis. We reveal that Jumonji domain-containing 4 (Jmjd4), a 2-oxoglutarate and Fe(II)-dependent oxygenase, catalyzes carbon 4 (C4) lysyl hydroxylation of eRF1. This posttranslational modification takes place at an invariant lysine within the eRF1 NIKS motif and is required for optimal translational termination efficiency. These findings further highlight the role of 2-oxoglutarate/Fe(II) oxygenases in fundamental cellular processes and provide additional evidence that ensuring fidelity of protein translation is a major role of hydroxylation.
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