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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.

Original publication




Journal article


Mol Cell

Publication Date





645 - 654


Amino Acid Sequence, Animals, Catalysis, Cell Line, Tumor, Codon, Terminator, Gene Expression Regulation, HeLa Cells, Histone Demethylases, Humans, Hydrolysis, Hydroxylation, Mixed Function Oxygenases, Models, Molecular, Molecular Sequence Data, Peptide Chain Termination, Translational, Peptide Termination Factors, Protein Biosynthesis, Protein Processing, Post-Translational, Protein Structure, Tertiary, Sequence Homology, Amino Acid