Negative catalysis by the editing domain of class I aminoacyl-tRNA synthetases
Author:
Affiliation:
1. Department of Chemistry, Faculty of Science, University of Zagreb, Zagreb 10000, Croatia
2. Institute for Clinical Sciences, Faculty of Medicine, Imperial College London and MRC London Institute of Medical Sciences, London, SW7 2AZ, UK
Abstract
Funder
Croatian Science Foundation
Swiss Enlargement Contribution in the framework of the Croatian-Swiss Research Programme
European Regional Development Fund
Publisher
Oxford University Press (OUP)
Subject
Genetics
Link
https://academic.oup.com/nar/article-pdf/50/7/4029/43402017/gkac207.pdf
Reference72 articles.
1. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs;Eriani;Nature,1990
2. Two classes of tRNA synthetases suggested by sterically compatible dockings on tRNA acceptor stem;Ribas de Pouplana;Cell,2001
3. Distinct kinetic mechanisms of the two classes of Aminoacyl-tRNA synthetases;Zhang;J. Mol. Biol.,2006
4. Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration;Lee;Nature,2006
5. The physiological target for LeuRS translational quality control is norvaline;Cvetesic;EMBO J,2014
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1. Gly56 in the synthetic site of isoleucyl‐tRNA synthetase confers specificity and maintains communication with the editing site;FEBS Letters;2023-12
2. A standalone editing protein deacylates mischarged canavanyl-tRNAArg to prevent canavanine incorporation into proteins;Nucleic Acids Research;2023-01-11
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