ArticleThe Journal of biological chemistry2012
Staphylococcus aureus CymR is a new thiol-based oxidation-sensing regulator of stress resistance and oxidative response.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 48 citations in OpenAlex.
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- Fe-S cluster homeostasis and beyond: The multifaceted roles of IscR.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Structural determinants of DNA recognition by the NO sensor NsrR and related Rrf2-type [FeS]-transcription factors.Communications biology · 2022Article
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- A Resourceful Race: Bacterial Scavenging of Host Sulfur Metabolism during Colonization.Infection and immunity · 2022Review
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- A compendium of DNA-binding specificities of transcription factors in Pseudomonas syringae.Nature communications · 2020Article
- Redox-Sensing Under Hypochlorite Stress and Infection Conditions by the Rrf2-Family Repressor HypR in Staphylococcus aureus.Antioxidants & redox signaling · 2018Article
- Identification of catabolite control protein A fromChemical science · 2017Article
- Novel Cysteine Desulfidase CdsB Involved in Releasing Cysteine Repression of Toxin Synthesis inFrontiers in cellular and infection microbiology · 2017Article
- Molecular Insights into the Impact of Oxidative Stress on the Quorum-Sensing Regulator Protein LasR.The Journal of biological chemistry · 2016Article
- Structure and mechanism of the essential two-component signal-transduction system WalKR in Staphylococcus aureus.Nature communications · 2016Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
As a human pathogen, Staphylococcus aureus must cope with oxidative stress generated by the human immune system. Here, we report that CymR utilizes its sole Cys-25 to sense oxidative stress. Oxidation followed by thiolation of this cysteine residue leads to dissociation of CymR from its cognate promoter DNA. In contrast, the DNA binding of the CymRC25S mutant was insensitive to oxidation and thiolation, suggesting that CymR senses oxidative stress through oxidation of its sole cysteine to form a mixed disulfide with low molecular weight thiols. The determined crystal structures of the reduced and oxidized forms of CymR revealed that Cys-25 is oxidized to Cys-25-SOH in the presence of H(2)O(2). Deletion of cymR reduced the resistance of S. aureus to oxidative stresses, and the resistance was restored by expressing a C25S mutant copy of cymR. In a C25S substitution mutant, the expression of two genes, tcyP and mccB, was constitutively repressed and did not respond to hydrogen peroxide stress, whereas the expression of the genes were highly induced under oxidative stress in a wild-type strain, indicating the critical role of Cys-25 in redox signaling in vivo. Thus, CymR is another master regulator that senses oxidative stress and connects stress responses to virulence regulation in S. aureus.
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