ArticleMolecular microbiology2022
Methionine oxidation under anaerobic conditions in Escherichia coli.
Article in Molecular microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Periplasmic detoxification of urate hydroperoxide underpinsbioRxiv : the preprint server for biology · 2026Article
- A short peptide derived from late embryogenesis abundant proteins enhances acid tolerance in Escherichia coli via modulation of two-component regulatory systems.The FEBS journal · 2026Article
- Repair of oxidized methionine residues in the chaperone Spy maintains periplasmic proteostasis under chlorite stress in Escherichia coli.PLoS biology · 2025Article
- The hallmarks of a tradeoff in transcriptomes that balances stress and growth functions.mSystems · 2024Article
- Article
- Identification of Antibacterial Components and Modes in the Methanol-Phase Extract from a Herbal PlantFoods (Basel, Switzerland) · 2023Article
- The hallmarks of a tradeoff in transcriptomes that balances stress and growth functions.Research square · 2023Article
- Methionine oxidation under anaerobic conditions in Escherichia coli.Molecular microbiology · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Repairing oxidative-targeted macromolecules is a central mechanism necessary for living organisms to adapt to oxidative stress. Reactive oxygen and chlorine species preferentially oxidize sulfur-containing amino acids in proteins. Among these amino acids, methionine can be converted into methionine sulfoxide. This post-translational oxidation can be reversed by methionine sulfoxide reductases, Msr enzymes. In Gram-negative bacteria, the antioxidant MsrPQ system is involved in the repair of periplasmic oxidized proteins. Surprisingly, in this study, we observed in Escherichia coli that msrPQ was highly expressed in the absence of oxygen. We have demonstrated that the anaerobic induction of msrPQ was due to chlorate (ClO
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