ArticleThe Journal of biological chemistry2014
A new role for Escherichia coli DsbC protein in protection against oxidative stress.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 33 citations in OpenAlex.
- Stable co-existence ofmBio · 2026Article
- Damage dynamics and the role of chance in the timing of E. coli cell death.Nature communications · 2023Article
- Enzymatic basis of the Fc-selective intra-chain disulfide reduction and free thiol content variability in an antibody produced in Escherichia coli.Microbial cell factories · 2022Article
- Genetic Determinants in Salmonella enterica Serotype Typhimurium Required for OvercomingMicrobiology spectrum · 2021Article
- Role of the Redox State of Human Peroxiredoxin-5 on Its TLR4-Activating DAMP Function.Antioxidants (Basel, Switzerland) · 2021Article
- Redox Protein OsaR (PA0056) RegulatesAntimicrobial agents and chemotherapy · 2021Article
- Complex Diffusion in Bacteria.Advances in experimental medicine and biology · 2020Review
- C8J_1298, a bifunctional thiol oxidoreductase of Campylobacter jejuni, affects Dsb (disulfide bond) network functioning.PloS one · 2020Article
- Disulfide Bond Formation in the Periplasm ofEcoSal Plus · 2019Review
- Oxidative stress, protein damage and repair in bacteria.Nature reviews. Microbiology · 2017Review
- Bacterial thiol oxidoreductases - from basic research to new antibacterial strategies.Applied microbiology and biotechnology · 2017Review
- Global Screening ofFrontiers in microbiology · 2017Article
- Sulfur Denitrosylation by an Engineered Trx-like DsbG Enzyme Identifies Nucleophilic Cysteine Hydrogen Bonds as Key Functional Determinant.The Journal of biological chemistry · 2016Article
- Converting a Sulfenic Acid Reductase into a Disulfide Bond Isomerase.Antioxidants & redox signaling · 2015Article
- Purification, crystallization and preliminary crystallographic investigation of FrnE, a disulfide oxidoreductase from Deinococcus radiodurans.Acta crystallographica. Section F, Structural biology communications · 2014Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
We report a new function for Escherichia coli DsbC, a protein best known for disulfide bond isomerization in the periplasm. We found that DsbC regulates the redox state of the single cysteine of the L-arabinose-binding protein AraF. This cysteine, which can be oxidized to a sulfenic acid, mediates the formation of a disulfide-linked homodimer under oxidative stress conditions, preventing L-arabinose binding. DsbC, unlike the homologous protein DsbG, reduces the intermolecular disulfide, restoring AraF binding properties. Thus, our results reveal a new link between oxidative protein folding and the defense mechanisms against oxidative stress.
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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.