ArticleMolecular microbiology2012
The auxiliary protein complex SaePQ activates the phosphatase activity of sensor kinase SaeS in the SaeRS two-component system of Staphylococcus aureus.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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70 citing papers in PubMed, 88 citations in OpenAlex.
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- A novel SaeS-targeting antivirulence antagonist screened against methicillin-resistantFrontiers in cellular and infection microbiology · 2026Article
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- Linking Virulence and Iron Limitation Response inJournal of proteome research · 2025Article
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- Antibacterial Effects of Synthetic Plantaricins AgainstAntibiotics (Basel, Switzerland) · 2025Article
- CodY controls the SaeR/S two-component system by modulating branched-chain fatty acid synthesis inJournal of bacteriology · 2024Article
- Staphylococcus aureus SaeRS impairs macrophage immune functions through bacterial clumps formation in the early stage of infection.NPJ biofilms and microbiomes · 2024Article
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- The Staphylococcus aureus CamS lipoprotein is a repressor of toxin production that shapes host-pathogen interaction.PLoS biology · 2024Article
- Review
- The Small Protein ScrA Influences Staphylococcus aureus Virulence-Related Processes via the SaeRS System.Microbiology spectrum · 2023Article
- A genetic regulatory see-saw of biofilm and virulence in MRSA pathogenesis.Frontiers in microbiology · 2023Review
- Computational tools for exploring peptide-membrane interactions in gram-positive bacteria.Computational and structural biotechnology journal · 2023Review
- A Review of Biofilm Formation ofAntibiotics (Basel, Switzerland) · 2022Review
- Regulation of the Sae Two-Component System by Branched-Chain Fatty Acids in Staphylococcus aureus.mBio · 2022Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
10 authors at 6 institutions in 1 country.
Funding
Abstract
In bacterial two-component regulatory systems (TCSs), dephosphorylation of phosphorylated response regulators is essential for resetting the activated systems to the pre-activation state. However, in the SaeRS TCS, a major virulence TCS of Staphylococcus aureus, the mechanism for dephosphorylation of the response regulator SaeR has not been identified. Here we report that two auxiliary proteins from the sae operon, SaeP and SaeQ, form a protein complex with the sensor kinase SaeS and activate the sensor kinase's phosphatase activity. Efficient activation of the phosphatase activity required the presence of both SaeP and SaeQ. When SaeP and SaeQ were ectopically expressed, the expression of coagulase, a sae target with low affinity for phosphorylated SaeR, was greatly reduced, while the expression of alpha-haemolysin, a sae target with high affinity for phosphorylated SaeR, was not, demonstrating a differential effect of SaePQ on sae target gene expression. When expression of SaePQ was abolished, most sae target genes were induced at an elevated level. Since the expression of SaeP and SaeQ is induced by the SaeRS TCS, these results suggest that the SaeRS TCS returns to the pre-activation state by a negative feedback mechanism.
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