ArticleFEMS microbiology letters2012
McsA and the roles of metal-binding motif in Staphylococcus aureus.
Article in FEMS microbiology letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- Complex structure and activation mechanism of arginine kinase McsB by McsA.Nature chemical biology · 2025Article
- Isolation of a novel multiple-heavy metal resistant Lampropedia aestuarii GYF-1 and investigation of its bioremediation potential.BMC microbiology · 2023Article
- Article
- Understanding Stress Response to High-Arsenic Gold-Bearing Sulfide Concentrate in Extremely Metal-Resistant AcidophileMicroorganisms · 2020Article
- The SAV1322 gene from Staphylococcus aureus: genomic and proteomic approaches to identification and characterization of gene function.BMC microbiology · 2016Article
- Role of adaptor TrfA and ClpPC in controlling levels of SsrA-tagged proteins and antitoxins in Staphylococcus aureus.Journal of bacteriology · 2014Article
- The mcsB gene of the clpC operon is required for stress tolerance and virulence in Staphylococcus aureus.Microbiology (Reading, England) · 2012Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
McsA is a key modulator of stress response in Staphylococcus aureus that contains four CXXC potential metal-binding motifs at the N-terminal. Staphylococcus aureus ctsR operon encodes ctsR, clpC, and putative mcsA and mcsB genes. The expression of the ctsR operon in S. aureus was shown to be induced in response to various types of heavy metals such as copper and cadmium. McsA was cloned and overexpressed, and purified product was tested for metal-binding activity. The protein bound to Cu(II), Zn(II), Co(II), and Cd(II). No binding with any heavy metal except copper was found when we performed site-directed mutagenesis of Cys residues of three CXXC motifs of McsA. These data suggest that two conserved cysteine ligands provided by one CXXC motif are required to bind copper ions. In addition, using a bacterial two-hybrid system, McsA was found to be able to bind to McsB and CtsR of S. aureus and the CXXC motif was needed for the binding. This indicates that the Cys residues in the CXXC motif are involved in metal binding and protein interaction.
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Registered trials
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