ArticleThe Journal of biological chemistry2009
Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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50 citing papers in PubMed, 88 citations in OpenAlex.
- PerR functions as a redox-sensing transcription factor regulating metal homeostasis in the thermoacidophilic archaeon Saccharolobus islandicus REY15A.Nucleic acids research · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
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- MRSA lineage USA300 isolated from bloodstream infections exhibit altered virulence regulation.Cell host & microbe · 2023Article
- Regulation of Staphylococcal Capsule by SarZ is SigA-Dependent.Journal of bacteriology · 2022Article
- The two-Cys-type TetR repressor GbaA confers resistance under disulfide and electrophile stress in Staphylococcus aureus.Free radical biology & medicine · 2021Article
- Redox regulation by reversible protein S-thiolation in Gram-positive bacteria.Redox biology · 2019Review
- OhsR acts as an organic peroxide-sensing transcriptional activator using an S-mycothiolation mechanism in Corynebacterium glutamicum.Microbial cell factories · 2018Article
- Redox-Sensing Under Hypochlorite Stress and Infection Conditions by the Rrf2-Family Repressor HypR in Staphylococcus aureus.Antioxidants & redox signaling · 2018Article
- Snapshots of C-S Cleavage in Egt2 Reveals Substrate Specificity and Reaction Mechanism.Cell chemical biology · 2018Article
- Determining the Roles of a Conserved α-Helix in a Global Virulence Regulator from Staphylococcus aureus.The protein journal · 2018Article
- Protein S-Bacillithiolation Functions in Thiol Protection and Redox Regulation of the Glyceraldehyde-3-Phosphate Dehydrogenase Gap in Staphylococcus aureus Under Hypochlorite Stress.Antioxidants & redox signaling · 2018Article
- The Role of Bacillithiol in Gram-Positive Firmicutes.Antioxidants & redox signaling · 2018Review
- The AGXX® Antimicrobial Coating Causes a Thiol-Specific Oxidative Stress Response and ProteinFrontiers in microbiology · 2018Article
- Redox-Sensitive MarR Homologue BifR from Burkholderia thailandensis Regulates Biofilm Formation.Biochemistry · 2017Article
- Neutrophil-generated oxidative stress and protein damage in Staphylococcus aureus.Pathogens and disease · 2016Review
- Impact of Environmental Cues on Staphylococcal Quorum Sensing and Biofilm Development.The Journal of biological chemistry · 2016Review
- A Surfactant-Induced Functional Modulation of a Global Virulence Regulator from Staphylococcus aureus.PloS one · 2016Article
- Crystallographic studies of SarV, a global regulator from Staphylococcus aureus.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Thiol-based redox switches in prokaryotes.Biological chemistry · 2015Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
SarZ is a global transcriptional regulator that uses a single cysteine residue, Cys(13), to sense peroxide stress and control metabolic switching and virulence in Staphylococcus aureus. SarZ belongs to the single-cysteine class of OhrR-MgrA proteins that play key roles in oxidative resistance and virulence regulation in various bacteria. We present the crystal structures of the reduced form, sulfenic acid form, and mixed disulfide form of SarZ. Both the sulfenic acid and mixed disulfide forms are structurally characterized for the first time for this class of proteins. The Cys(13) sulfenic acid modification is stabilized through two hydrogen bonds with surrounding residues, and the overall DNA-binding conformation is retained. A further reaction of the Cys(13) sulfenic acid with an external thiol leads to formation of a mixed disulfide bond, which results in an allosteric change in the DNA-binding domains, disrupting DNA binding. Thus, the crystal structures of SarZ in three different states provide molecular level pictures delineating the mechanism by which this class of redox active regulators undergoes activation. These structures help to understand redox-mediated virulence regulation in S. aureus and activation of the MarR family proteins in general.
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