ArticleJournal of bacteriology2010
In the Staphylococcus aureus two-component system sae, the response regulator SaeR binds to a direct repeat sequence and DNA binding requires phosphorylation by the sensor kinase SaeS.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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Who cites it
86 citing papers in PubMed.
- Article
- Elucidating the Staphylococcus aureus TSST-1 Regulatory Network as a Response to Vaginal pH.Molecular microbiology · 2026Article
- Antibacterial and anti-virulence activity of the repurposed agent SX-682 against Staphylococcus aureus.BMC microbiology · 2026Article
- A novel SaeS-targeting antivirulence antagonist screened against methicillin-resistantFrontiers in cellular and infection microbiology · 2026Article
- Article
- Article
- Pyrimidine sufficiency is required for Sae two-component system signaling inJournal of bacteriology · 2025Article
- Environmental cues in different host niches shape the survival fitness of Staphylococcus aureus.Nature communications · 2025Article
- Linking Virulence and Iron Limitation Response inJournal of proteome research · 2025Article
- AACS synthetic biology · 2025Article
- Baohuoside I targets SaeR as an antivirulence strategy to disrupt MRSA biofilm formation and pathogenicity.NPJ biofilms and microbiomes · 2025Article
- YjbH contributes toVirulence · 2024Article
- CodY controls the SaeR/S two-component system by modulating branched-chain fatty acid synthesis inJournal of bacteriology · 2024Article
- Discovery of an antivirulence compound that targets the Staphylococcus aureus SaeRS two-component system to inhibit toxic shock syndrome toxin-1 production.The Journal of biological chemistry · 2024Article
- A comprehensive analysis of pneumococcal two-component system regulatory networks.NAR genomics and bioinformatics · 2024Article
- The Application of Rat Models inPathogens (Basel, Switzerland) · 2024Review
- The Staphylococcus aureus CamS lipoprotein is a repressor of toxin production that shapes host-pathogen interaction.PLoS biology · 2024Article
- SaeR as a novel target for antivirulence therapy againstEmerging microbes & infections · 2023Article
- Diabetes mellitus promotes the nasal colonization of high virulentEmerging microbes & infections · 2023Article
- Complex Regulation of Gamma-Hemolysin Expression Impacts Staphylococcus aureus Virulence.Microbiology spectrum · 2023Article
26 more citing papers are in PubMed but not listed here.
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6 authors.
Funding
Abstract
Staphylococcus aureus uses the SaeRS two-component system to control the expression of many virulence factors such as alpha-hemolysin and coagulase; however, the molecular mechanism of this signaling has not yet been elucidated. Here, using the P1 promoter of the sae operon as a model target DNA, we demonstrated that the unphosphorylated response regulator SaeR does not bind to the P1 promoter DNA, while its C-terminal DNA binding domain alone does. The DNA binding activity of full-length SaeR could be restored by sensor kinase SaeS-induced phosphorylation. Phosphorylated SaeR is more resistant to digestion by trypsin, suggesting conformational changes. DNase I footprinting assays revealed that the SaeR protection region in the P1 promoter contains a direct repeat sequence (GTTAAN(6)GTTAA [where N is any nucleotide]). This sequence is critical to the binding of phosphorylated SaeR. Mutational changes in the repeat sequence greatly reduced both the in vitro binding of SaeR and the in vivo function of the P1 promoter. From these results, we concluded that SaeR recognizes the direct repeat sequence as a binding site and that binding requires phosphorylation by SaeS.
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