ArticleJournal of bacteriology2006
Phosphorylation of the group A Streptococcal CovR response regulator causes dimerization and promoter-specific recruitment by RNA polymerase.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 58 citations in OpenAlex.
- Molecular Characterization of the Group A Streptococcus Virulence-Regulatory System FasBCAX.Molecular microbiology · 2025Article
- Repurposing Diflunisal as an Antivirulence Agent AgainstInfectious microbes & diseases · 2025Article
- Characterization of a novelmBio · 2025Article
- Hyperphosphorylation of the Group A Streptococcal Control of Virulence Regulator Increases Promoter Occupancy Specifically at Virulence Factor-Encoding Genes.Journal of bacteriology · 2023Article
- RopB represses the transcription ofLife science alliance · 2023Article
- A Novel CovS Variant Harbored by a Colonization Strain Reduces Streptococcus pyogenes Virulence.Journal of bacteriology · 2023Article
- Article
- CovS inactivation reduces CovR promoter binding at diverse virulence factor encoding genes in group A Streptococcus.PLoS pathogens · 2022Article
- Genetic Basis Underlying the Hyperhemolytic Phenotype of Streptococcus agalactiae Strain CNCTC10/84.Journal of bacteriology · 2020Article
- The group A Streptococcus accessory protein RocA: regulatory activity, interacting partners and influence on disease potential.Molecular microbiology · 2020Article
- Phosphatase activity of the control of virulence sensor kinase CovS is critical for the pathogenesis of group A streptococcus.PLoS pathogens · 2018Article
- Role of CovR phosphorylation in gene transcription in Streptococcus mutans.Microbiology (Reading, England) · 2018Article
- Use of a Phosphorylation Site Mutant To Identify Distinct Modes of Gene Repression by the Control of Virulence Regulator (CovR) in Streptococcus pyogenes.Journal of bacteriology · 2017Article
- Regulatory gene mutation: a driving force behind group a Streptococcus strain- and serotype-specific variation.Molecular microbiology · 2017Review
- Two-component signal transduction systems in oral bacteria.Journal of oral microbiology · 2017Review
- Null Mutations of Group A Streptococcus Orphan Kinase RocA: Selection in Mouse Infection and Comparison with CovS Mutations in Alteration of In Vitro and In Vivo Protease SpeB Expression and Virulence.Infection and immunity · 2017Article
- Pyruvate Oxidase as a Critical Link between Metabolism and Capsule Biosynthesis in Streptococcus pneumoniae.PLoS pathogens · 2016Article
- Repression of Rgg But Not Upregulation of LacD.1 inFrontiers in microbiology · 2016Article
- Regulatory rewiring confers serotype-specific hyper-virulence in the human pathogen group A Streptococcus.Molecular microbiology · 2015Article
- Characterization of the effect of the histidine kinase CovS on response regulator phosphorylation in group A Streptococcus.Infection and immunity · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The group A streptococcus (GAS), Streptococcus pyogenes, is an important human pathogen that causes infections ranging in severity from self-limiting pharyngitis to severe invasive diseases that are associated with significant morbidity and mortality. The pathogenic effects of GAS are mediated by the expression of virulence factors, one of which is the hyaluronic acid capsule (encoded by genes in the has operon). The expression of these virulence factors is controlled by the CovR/S (CsrR/S) two-component regulatory system of GAS which regulates, directly or indirectly, the expression of about 15% of the genome. CovR is a member of the OmpR/PhoB family of transcriptional regulators. Here we show that phosphorylation by acetyl phosphate results in dimerization of CovR. Dimerization was not observed using a D53A mutant of CovR, indicating that D53 is the site of phosphorylation in CovR. Phosphorylation stimulated binding of CovR to a DNA fragment containing the promoter of the has operon (Phas) approximately twofold. Binding of CovR D53A mutant protein to Phas was indistinguishable from the binding of wild-type unphosphorylated CovR. In vitro transcription, using purified GAS RNA polymerase, showed that wild-type CovR repressed transcription, and repression was stimulated more than sixfold by phosphorylation. In the presence of RNA polymerase, binding at Phas of phosphorylated, but not unphosphorylated, CovR was stimulated about fourfold, which accounts for the difference in the effect of phosphorylation on repression versus DNA binding. Thus, regulation of Phas by CovR is direct, and the degree of repression of Phas is controlled by the phosphorylation of CovR.
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