ArticleAntioxidants & redox signaling2013
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Article in Antioxidants & redox signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 91 citations in OpenAlex.
- The methyltransferase NmbA methylates the low-molecular weight thiol bacillithiol, and displays a specific structural architecture.Redox biology · 2025Article
- In Silico Safety Assessment ofInternational journal of molecular sciences · 2024Article
- Sulfinamide Formation from the Reaction of Bacillithiol and Nitroxyl.ACS chemical biology · 2023Article
- MarR Family Transcriptional Regulators and Their Roles in Plant-Interacting Bacteria.Microorganisms · 2023Review
- Glyoxalase 2: Towards a Broader View of the Second Player of the Glyoxalase System.Antioxidants (Basel, Switzerland) · 2022Review
- 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
- The two-Cys-type TetR repressor GbaA confers resistance under disulfide and electrophile stress in Staphylococcus aureus.Free radical biology & medicine · 2021Article
- Redox proteomic study of Bacillus cereus thiol proteome during fermentative anaerobic growth.BMC genomics · 2021Article
- Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities.Redox biology · 2021Review
- The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr (YpdA) disulfide reductase reduce S-bacillithiolated proteins.Redox biology · 2021Article
- Underground metabolism facilitates the evolution of novel pathways for vitamin B6 biosynthesis.Applied microbiology and biotechnology · 2021Review
- Article
- Nitric oxide disrupts bacterial cytokinesis by poisoning purine metabolism.Science advances · 2020Article
- Method for measurement of bacillithiol redox potential changes using the Brx-roGFP2 redox biosensor inMethodsX · 2020Article
- The Disulfide Stress Response and ProteinAntioxidants (Basel, Switzerland) · 2019Article
- YpdA, a putative bacillithiol disulfide reductase, contributes to cellular redox homeostasis and virulence in Staphylococcus aureus.Molecular microbiology · 2019Article
- Article
- Glyceraldehyde-3-phosphate dehydrogenase fromFEBS open bio · 2019Article
- Redox regulation by reversible protein S-thiolation in Gram-positive bacteria.Redox biology · 2019Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
aimsProtein S-bacillithiolations are mixed disulfides between protein thiols and the bacillithiol (BSH) redox buffer that occur in response to NaOCl in Bacillus subtilis. We used BSH-specific immunoblots, shotgun liquid chromatography (LC)-tandem mass spectrometry (MS/MS) analysis and redox proteomics to characterize the S-bacillithiolomes of B. subtilis, B. megaterium, B. pumilus, B. amyloliquefaciens, and Staphylococcus carnosus and also measured the BSH/oxidized bacillithiol disulfide (BSSB) redox ratio after NaOCl stress.
resultsIn total, 54 proteins with characteristic S-bacillithiolation (SSB) sites were identified, including 29 unique proteins and eight proteins conserved in two or more of these bacteria. The methionine synthase MetE is the most abundant S-bacillithiolated protein in Bacillus species after NaOCl exposure. Further, S-bacillithiolated proteins include the translation elongation factor EF-Tu and aminoacyl-tRNA synthetases (ThrS), the DnaK and GrpE chaperones, the two-Cys peroxiredoxin YkuU, the ferredoxin-NADP(+) oxidoreductase YumC, the inorganic pyrophosphatase PpaC, the inosine-5'-monophosphate dehydrogenase GuaB, proteins involved in thiamine biosynthesis (ThiG and ThiM), queuosine biosynthesis (QueF), biosynthesis of aromatic amino acids (AroA and AroE), serine (SerA), branched-chain amino acids (YwaA), and homocysteine (LuxS and MetI). The thioredoxin-like proteins, YphP and YtxJ, are S-bacillithiolated at their active sites, suggesting a function in the de-bacillithiolation process. S-bacillithiolation is accompanied by a two-fold increase in the BSSB level and a decrease in the BSH/BSSB redox ratio in B. subtilis. INNOVATION: Many essential and conserved proteins, including the dominant MetE, were identified in the S-bacillithiolome of different Bacillus species and S. carnosus using shotgun-LC-MS/MS analyses.
conclusionS-bacillithiolation is a widespread redox control mechanism among Firmicutes bacteria that protects conserved metabolic enzymes and essential proteins against overoxidation.
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