Imperial College London
Alternate

Dr Luke A. Yates

Faculty of Medicine, Department of Infectious Disease

Research Associate
 
 
 
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Contact

 

luke.yates

 
 
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Location

 

245Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Feng:2014:10.1016/j.molcel.2013.12.028,
author = {Feng, T and Yamamoto, A and Wilkins, SE and Sokolova, E and Yates, LA and Münzel, M and Singh, P and Hopkinson, RJ and Fischer, R and Cockman, ME and Shelley, J and Trudgian, DC and Schödel, J and McCullagh, JSO and Ge, W and Kessler, BM and Gilbert, RJ and Frolova, LY and Alkalaeva, E and Ratcliffe, PJ and Schofield, CJ and Coleman, ML},
doi = {10.1016/j.molcel.2013.12.028},
journal = {Mol Cell},
pages = {645--654},
title = {Optimal translational termination requires C4 lysyl hydroxylation of eRF1.},
url = {http://dx.doi.org/10.1016/j.molcel.2013.12.028},
volume = {53},
year = {2014}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - 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.
AU  - Feng,T
AU  - Yamamoto,A
AU  - Wilkins,SE
AU  - Sokolova,E
AU  - Yates,LA
AU  - Münzel,M
AU  - Singh,P
AU  - Hopkinson,RJ
AU  - Fischer,R
AU  - Cockman,ME
AU  - Shelley,J
AU  - Trudgian,DC
AU  - Schödel,J
AU  - McCullagh,JSO
AU  - Ge,W
AU  - Kessler,BM
AU  - Gilbert,RJ
AU  - Frolova,LY
AU  - Alkalaeva,E
AU  - Ratcliffe,PJ
AU  - Schofield,CJ
AU  - Coleman,ML
DO  - 10.1016/j.molcel.2013.12.028
EP  - 654
PY  - 2014///
SP  - 645
TI  - Optimal translational termination requires C4 lysyl hydroxylation of eRF1.
T2  - Mol Cell
UR  - http://dx.doi.org/10.1016/j.molcel.2013.12.028
UR  - https://www.ncbi.nlm.nih.gov/pubmed/24486019
VL  - 53
ER  -
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