ArticleNucleic acids research2014
Mechanism of oxidant-induced mistranslation by threonyl-tRNA synthetase.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 44 citations in OpenAlex.
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- A metal ion mediated functional dichotomy encodes plasticity during translation quality control.Nature communications · 2025Article
- Interplay between mistranslation and oxidative stress inArhiv za higijenu rada i toksikologiju · 2024Article
- Article
- The central role of translation elongation in response to stress.Biochemical Society transactions · 2023Article
- Translational Fidelity during Bacterial Stresses and Host Interactions.Pathogens (Basel, Switzerland) · 2023Review
- Comparative pangenomics: analysis of 12 microbial pathogen pangenomes reveals conserved global structures of genetic and functional diversity.BMC genomics · 2022Article
- Oxidative stress strongly restricts the effect of codon choice on the efficiency of protein synthesis inFrontiers in microbiology · 2022Article
- Oxidation alters the architecture of the phenylalanyl-tRNA synthetase editing domain to confer hyperaccuracy.Nucleic acids research · 2021Article
- Oxidative Stress in Bacteria and the Central Dogma of Molecular Biology.Frontiers in molecular biosciences · 2021Review
- Integrated Redox Proteomic Analysis Highlights New Mechanisms of Sensitivity to Silver Nanoparticles.Molecular & cellular proteomics : MCP · 2021Article
- Nitrosative stress inhibits aminoacylation and editing activities of mitochondrial threonyl-tRNA synthetase by S-nitrosation.Nucleic acids research · 2020Article
- Modulation ofFrontiers in genetics · 2020Article
- Modulating Mistranslation Potential of tRNAGenetics · 2019Article
- Oxidation of phenylalanyl-tRNA synthetase positively regulates translational quality control.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Pathways to disease from natural variations in human cytoplasmic tRNAs.The Journal of biological chemistry · 2019Review
- 11th IUBMB Focused Meeting on the Aminoacyl-tRNA Synthetases: Sailing a New Sea of Complex Functions in Human Biology and Disease.Biomolecules · 2018Article
- MS-READ: Quantitative measurement of amino acid incorporation.Biochimica et biophysica acta. General subjects · 2017Article
- Rewiring protein synthesis: From natural to synthetic amino acids.Biochimica et biophysica acta. General subjects · 2017Review
- Translational fidelity and mistranslation in the cellular response to stress.Nature microbiology · 2017Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminoacyl-tRNA synthetases maintain the fidelity during protein synthesis by selective activation of cognate amino acids at the aminoacylation site and hydrolysis of misformed aminoacyl-tRNAs at the editing site. Threonyl-tRNA synthetase (ThrRS) misactivates serine and utilizes an editing site cysteine (C182 in Escherichia coli) to hydrolyze Ser-tRNA(Thr). Hydrogen peroxide oxidizes C182, leading to Ser-tRNA(Thr) production and mistranslation of threonine codons as serine. The mechanism of C182 oxidation remains unclear. Here we used a chemical probe to demonstrate that C182 was oxidized to sulfenic acid by air, hydrogen peroxide and hypochlorite. Aminoacylation experiments in vitro showed that air oxidation increased the Ser-tRNA(Thr) level in the presence of elongation factor Tu. C182 forms a putative metal binding site with three conserved histidine residues (H73, H77 and H186). We showed that H73 and H186, but not H77, were critical for activating C182 for oxidation. Addition of zinc or nickel ions inhibited C182 oxidation by hydrogen peroxide. These results led us to propose a model for C182 oxidation, which could serve as a paradigm for the poorly understood activation mechanisms of protein cysteine residues. Our work also suggests that bacteria may use ThrRS editing to sense the oxidant levels in the environment.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.