ArticleAntioxidants & redox signaling2018
Protein S-Bacillithiolation Functions in Thiol Protection and Redox Regulation of the Glyceraldehyde-3-Phosphate Dehydrogenase Gap in Staphylococcus aureus Under Hypochlorite Stress.
Article in Antioxidants & redox signaling, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 58 citations in OpenAlex.
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- The Catalase KatA Contributes to Microaerophilic HAntioxidants (Basel, Switzerland) · 2022Article
- Profiling the Site of Protein CoAlation and Coenzyme A Stabilization Interactions.Antioxidants (Basel, Switzerland) · 2022Article
- Suppression of Thiol-Dependent Antioxidant System and Stress Response in Methicillin-Resistant Staphylococcus aureus by Docosanol: Explication Through Proteome Investigation.Molecular biotechnology · 2022Article
- Thiol Reductases inAntioxidants (Basel, Switzerland) · 2022Review
- 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
- An overview of moonlighting proteins in Staphylococcus aureus infection.Archives of microbiology · 2021Review
- The Writers, Readers, and Erasers in Redox Regulation of GAPDH.Antioxidants (Basel, Switzerland) · 2020Review
- Redefining the Clostridioides difficile σmSphere · 2020Article
- Identification of Bacterial Protein Interaction Partners Points to New Intracellular Functions ofFrontiers in microbiology · 2020Article
- The Disulfide Stress Response and ProteinAntioxidants (Basel, Switzerland) · 2019Article
- The role of thiols in antioxidant systems.Free radical biology & medicine · 2019Review
- YpdA, a putative bacillithiol disulfide reductase, contributes to cellular redox homeostasis and virulence in Staphylococcus aureus.Molecular microbiology · 2019Article
- Article
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Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
Abstract
aimsBacillithiol (BSH) is the major low-molecular-weight thiol of the human pathogen Staphylococcus aureus. In this study, we used OxICAT and Voronoi redox treemaps to quantify hypochlorite-sensitive protein thiols in S. aureus USA300 and analyzed the role of BSH in protein S-bacillithiolation.
resultsThe OxICAT analyses enabled the quantification of 228 Cys residues in the redox proteome of S. aureus USA300. Hypochlorite stress resulted in >10% increased oxidation of 58 Cys residues (25.4%) in the thiol redox proteome. Among the highly oxidized sodium hypochlorite (NaOCl)-sensitive proteins are five S-bacillithiolated proteins (Gap, AldA, GuaB, RpmJ, and PpaC). The glyceraldehyde-3-phosphate (G3P) dehydrogenase Gap represents the most abundant S-bacillithiolated protein contributing 4% to the total Cys proteome. The active site Cys151 of Gap was very sensitive to overoxidation and irreversible inactivation by hydrogen peroxide (H
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