Optimal Translational Termination Requires C4 Lysyl Hydroxylation of eRF1

• DOI: 10.1016/j.molcel.2013.12.028
• Publication Date: 2014-01-31T07:46:03Z
• Authors: Tianshu Feng; Atsushi Yamamoto; Sarah E. Wilkins; Elizaveta Sokolova; Luke A. Yates; Martin Münzel; Pooja Singh; Richard J. Hopkinson; Roman Fischer; Matthew E. Cockman; Jake Shelley; David C. Trudgian; Johannes Schödel; James S.O. McCullagh; Wei Ge; Benedikt M. Kessler; Robert J. Gilbert; Ludmila Y. Frolova; Elena Alkalaeva; Peter J. Ratcliffe; Christopher J. Sc...; Mathew L. Coleman
• Keywords: Hydroxylation; Release factor; Stop codon

Efficient stop codon recognition and peptidyl-tRNA hydrolysis are essential in order to terminate translational elongation maintain protein sequence fidelity. Eukaryotic termination is mediated by a release factor complex that includes eukaryotic 1 (eRF1) eRF3. The N terminus of eRF1 contains highly conserved motifs couple at the ribosomal A site hydrolysis. We reveal Jumonji domain-containing 4 (Jmjd4), 2-oxoglutarate- Fe(II)-dependent oxygenase, catalyzes carbon (C4) lysyl hydroxylation eRF1. This posttranslational modification takes place an invariant lysine within NIKS motif required for optimal efficiency. These findings further highlight role 2-oxoglutarate/Fe(II) oxygenases fundamental cellular processes provide additional evidence ensuring fidelity translation major hydroxylation.