ArticleAntioxidants & redox signaling2014
Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and MetE.
Article in Antioxidants & redox signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Integrated Optimization, Genomic Characterization, and Functional Evaluation of Biogenic Selenium Nanoparticles fromInternational journal of molecular sciences · 2026Article
- The methyltransferase NmbA methylates the low-molecular weight thiol bacillithiol, and displays a specific structural architecture.Redox biology · 2025Article
- Reductive activation of the disulfide-containing antibiotic thiolutin is mediated by both bacillithiol and FAD-dependent disulfide reductases.Journal of bacteriology · 2025Article
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- X-ray-driven chemistry and conformational heterogeneity in atomic resolution crystal structures of bacterial dihydrofolate reductases.bioRxiv : the preprint server for biology · 2023Article
- Suppression of Thiol-Dependent Antioxidant System and Stress Response in Methicillin-Resistant Staphylococcus aureus by Docosanol: Explication Through Proteome Investigation.Molecular biotechnology · 2022Article
- Structure of BrxA from Staphylococcus aureus, a bacilliredoxin involved in redox homeostasis in Firmicutes.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022Review
- OhrR is a central transcriptional regulator of virulence in Dickeya zeae.Molecular plant pathology · 2022Article
- Atypical Bacilliredoxin AbxC Plays a Role in Responding to Oxidative Stress in Radiation-Resistant BacteriumAntioxidants (Basel, Switzerland) · 2021Article
- The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr (YpdA) disulfide reductase reduce S-bacillithiolated proteins.Redox biology · 2021Article
- Carbon Source-Dependent Reprogramming of Anaerobic Metabolism in Staphylococcus aureus.Journal of bacteriology · 2021Article
- Article
- In Vivo Imaging with Genetically Encoded Redox Biosensors.International journal of molecular sciences · 2020Review
- Redox and Thiols in Archaea.Antioxidants (Basel, Switzerland) · 2020Review
- Oxidative Stress-Generating Antimicrobials, a Novel Strategy to Overcome Antibacterial Resistance.Antioxidants (Basel, Switzerland) · 2020Review
- Bacillus subtilis Regulators MntR and Zur Participate in Redox Cycling, Antibiotic Sensitivity, and Cell Wall Plasticity.Journal of bacteriology · 2020Article
- The Disulfide Stress Response and ProteinAntioxidants (Basel, Switzerland) · 2019Article
- Cross Talk between SigB and PrfA in Listeria monocytogenes Facilitates Transitions between Extra- and Intracellular Environments.Microbiology and molecular biology reviews : MMBR · 2019Review
- The role of thiols in antioxidant systems.Free radical biology & medicine · 2019Review
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Authors and funding
7 authors.
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Abstract
aimsIn bacillithiol (BSH)-utilizing organisms, protein S-bacillithiolation functions as a redox switch in response to oxidative stress and protects critical Cys residues against overoxidation. In Bacillus subtilis, both the redox-sensing repressor OhrR and the methionine synthase MetE are redox controlled by S-bacillithiolation in vivo. Here, we identify pathways of protein de-bacillithiolation and test the hypothesis that YphP(BrxA) and YqiW(BrxB) act as bacilliredoxins (Brx) to remove BSH from OhrR and MetE mixed disulfides.
resultsWe present evidence that the BrxA and BrxB paralogs have de-bacillithiolation activity. This Brx activity results from attack of the amino-terminal Cys residue in a CGC motif on protein BSH-mixed disulfides. B. subtilis OhrR DNA-binding activity is eliminated by S-thiolation on its sole Cys residue. Both the BrxA and BrxB bacilliredoxins mediate de-bacillithiolation of OhrR accompanied by the transfer of BSH to the amino-terminal cysteine of their CGC active site motif. In vitro studies demonstrate that BrxB can restore DNA-binding activity to OhrR which is S-bacillithiolated, but not to OhrR that is S-cysteinylated. MetE is most strongly S-bacillithiolated at Cys719 in vitro and can be efficiently de-bacillithiolated by both BrxA and BrxB. INNOVATION AND
conclusionWe demonstrate that BrxA and BrxB function in the reduction of BSH mixed protein disulfides with two natural substrates (MetE, OhrR). These results provide biochemical evidence for a new class of bacterial redox-regulatory proteins, the bacilliredoxins, which function analogously to glutaredoxins. Bacilliredoxins function in concert with other thiol-disulfide oxidoreductases to maintain redox homeostasis in response to disulfide stress conditions.
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