ArticleThe Journal of biological chemistry2015
Staphylococcus aureus PerR Is a Hypersensitive Hydrogen Peroxide Sensor using Iron-mediated Histidine Oxidation.
Article in The Journal of biological chemistry, 2015. 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.
- The oxidative stress regulator, PerR, is required for staphyloferrin B-mediated iron acquisition inJournal of bacteriology · 2026Article
- Integrated multi-omics reveals coordinatedmSystems · 2026Article
- Article
- Linking Virulence and Iron Limitation Response inJournal of proteome research · 2025Article
- Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Article
- Oxidative stress is intrinsic to staphylococcal adaptation to fatty acid synthesis antibiotics.iScience · 2024Article
- Article
- The Arsenal ofAntioxidants (Basel, Switzerland) · 2023Review
- Iron homeostasis inMicrobiology (Reading, England) · 2023Article
- The Catalase KatA Contributes to Microaerophilic HAntioxidants (Basel, Switzerland) · 2022Article
- Allicin, the Odor of Freshly Crushed Garlic: A Review of Recent Progress in Understanding Allicin's Effects on Cells.Molecules (Basel, Switzerland) · 2021Review
- Staphylococcus aureus induces an itaconate-dominated immunometabolic response that drives biofilm formation.Nature communications · 2021Article
- Article
- How Microbes Defend Themselves From Incoming Hydrogen Peroxide.Frontiers in immunology · 2021Review
- Genetic Regulation of Metal Ion Homeostasis in Staphylococcus aureus.Trends in microbiology · 2020Review
- Bacillus subtilis Fur Is a Transcriptional Activator for the PerR-RepressedJournal of bacteriology · 2020Article
- Redox Sensing by FeAntioxidants & redox signaling · 2018Review
- Spectral Library Based Analysis of Arginine Phosphorylations inMolecular & cellular proteomics : MCP · 2018Article
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Authors and funding
9 authors.
Funding
Abstract
In many Gram-positive bacteria PerR is a major peroxide sensor whose repressor activity is dependent on a bound metal cofactor. The prototype for PerR sensors, the Bacillus subtilis PerRBS protein, represses target genes when bound to either Mn(2+) or Fe(2+) as corepressor, but only the Fe(2+)-bound form responds to H2O2. The orthologous protein in the human pathogen Staphylococcus aureus, PerRSA, plays important roles in H2O2 resistance and virulence. However, PerRSA is reported to only respond to Mn(2+) as corepressor, which suggests that it might rely on a distinct, iron-independent mechanism for H2O2 sensing. Here we demonstrate that PerRSA uses either Fe(2+) or Mn(2+) as corepressor, and that, like PerRBS, the Fe(2+)-bound form of PerRSA senses physiological levels of H2O2 by iron-mediated histidine oxidation. Moreover, we show that PerRSA is poised to sense very low levels of endogenous H2O2, which normally cannot be sensed by B. subtilis PerRBS. This hypersensitivity of PerRSA accounts for the apparent lack of Fe(2+)-dependent repressor activity and consequent Mn(2+)-specific repressor activity under aerobic conditions. We also provide evidence that the activity of PerRSA is directly correlated with virulence, whereas it is inversely correlated with H2O2 resistance, suggesting that PerRSA may be an attractive target for the control of S. aureus pathogenesis.
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