ArticleThe Journal of biological chemistry2016
Oxidation of a Cysteine Residue in Elongation Factor EF-Tu Reversibly Inhibits Translation in the Cyanobacterium Synechocystis sp. PCC 6803.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 49 citations in OpenAlex.
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- Bacteriostatic Mechanism of the Ethyl Acetate Extract from the Root ofVeterinary sciences · 2026Article
- From photosynthetic electron flow to gene regulation: redox signal transduction in cyanobacteria.FEMS microbiology reviews · 2026Review
- Nitrogen limitation causes a seismic shift in redox state and phosphorylation of proteins implicated in carbon flux and lipidome remodeling in Rhodotorula toruloides.Biotechnology for biofuels and bioproducts · 2025Article
- Thioredoxin A regulates protein synthesis to maintain carbon and nitrogen partitioning in cyanobacteria.Plant physiology · 2024Article
- Chloroplast translation factor EF-Tu of Arabidopsis thaliana can be inactivated via oxidation of a specific cysteine residue.The Biochemical journal · 2023Article
- The ribosome assembly GTPase EngA is involved in redox signaling in cyanobacteria.Frontiers in microbiology · 2023Article
- Exploring the Diversity of the Thioredoxin Systems in Cyanobacteria.Antioxidants (Basel, Switzerland) · 2022Review
- Oxidative stress strongly restricts the effect of codon choice on the efficiency of protein synthesis inFrontiers in microbiology · 2022Article
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- Oxidative Stress in Bacteria and the Central Dogma of Molecular Biology.Frontiers in molecular biosciences · 2021Review
- Oxygen and ROS in Photosynthesis.Plants (Basel, Switzerland) · 2020Review
- Modulation ofFrontiers in genetics · 2020Article
- Elevated Levels of Specific Carotenoids During Acclimation to Strong Light Protect the Repair of Photosystem II inFrontiers in plant science · 2020Article
- Identification of Sulfenylated Cysteines inFrontiers in plant science · 2020Article
- Responses of Membranes and the Photosynthetic Apparatus to Salt Stress in Cyanobacteria.Frontiers in plant science · 2020Review
- Light-inducible expression of translation factor EF-Tu during acclimation to strong light enhances the repair of photosystem II.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Universal Molecular Triggers of Stress Responses in CyanobacteriumLife (Basel, Switzerland) · 2019Review
- Oxidation of Translation Factor EF-Tu Inhibits the Repair of Photosystem II.Plant physiology · 2018Article
- Light-controlled motility in prokaryotes and the problem of directional light perception.FEMS microbiology reviews · 2017Review
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translational elongation is susceptible to inactivation by reactive oxygen species (ROS) in the cyanobacterium Synechocystis sp. PCC 6803, and elongation factor G has been identified as a target of oxidation by ROS. In the present study we examined the sensitivity to oxidation by ROS of another elongation factor, EF-Tu. The structure of EF-Tu changes dramatically depending on the bound nucleotide. Therefore, we investigated the sensitivity to oxidation in vitro of GTP- and GDP-bound EF-Tu as well as that of nucleotide-free EF-Tu. Assays of translational activity with a reconstituted translation system from Escherichia coli revealed that GTP-bound and nucleotide-free EF-Tu were sensitive to oxidation by H2O2, whereas GDP-bound EF-Tu was resistant to H2O2. The inactivation of EF-Tu was the result of oxidation of Cys-82, a single cysteine residue, and subsequent formation of both an intermolecular disulfide bond and sulfenic acid. Replacement of Cys-82 with serine rendered EF-Tu resistant to inactivation by H2O2, confirming that Cys-82 was a target of oxidation. Furthermore, oxidized EF-Tu was reduced and reactivated by thioredoxin. Gel-filtration chromatography revealed that some of the oxidized nucleotide-free EF-Tu formed large complexes of >30 molecules. Atomic force microscopy revealed that such large complexes dissociated into several smaller aggregates upon the addition of dithiothreitol. Immunological analysis of the redox state of EF-Tu in vivo showed that levels of oxidized EF-Tu increased under strong light. Thus, resembling elongation factor G, EF-Tu appears to be sensitive to ROS via oxidation of a cysteine residue, and its inactivation might be reversed in a redox-dependent manner.
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