ArticleMolecular microbiology2020
Host stimuli and operator binding sites controlling protein interactions between virulence master regulator ToxR and ToxS in Vibrio cholerae.
Article in Molecular microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- Expression of Cholera Toxin (CT) and the Toxin Co-Regulated Pilus (TCP) by Variants of ToxT inToxins · 2023Article
- Holistic analysis of lysine acetylation in aquaculture pathogenic bacteriaFrontiers in veterinary science · 2023Article
- Co-component signal transduction systems: Fast-evolving virulence regulation cassettes discovered in enteric bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Bile Salts Promote ToxR Regulon Activation during Growth under Virulence-Inducing Conditions.Infection and immunity · 2021Article
- Vibrio cholerae TolC Is Required for Expression of the ToxR Regulon.Infection and immunity · 2021Article
- PsaF Is a Membrane-Localized pH Sensor That RegulatesJournal of bacteriology · 2021Article
- The periplasmic domains of Vibriocholerae ToxR and ToxS are forming a strong heterodimeric complex independent on the redox state of ToxR cysteines.Molecular microbiology · 2021Article
- σMolecular microbiology · 2021Article
- Assessment and Antibiotic Resistance Profiling inAntibiotics (Basel, Switzerland) · 2021Article
- Pathogenicity and virulence regulation ofVirulence · 2020Review
- Host stimuli and operator binding sites controlling protein interactions between virulence master regulator ToxR and ToxS in Vibrio cholerae.Molecular microbiology · 2020Article
- A disulfide constrains the ToxR periplasmic domain structure, altering its interactions with ToxS and bile-salts.Scientific reports · 2020Article
- The Interface ofGut microbesReview
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Protein-protein interactions (PPIs) are key mechanisms in the maintenance of biological regulatory networks. Herein, we characterize PPIs within ToxR and its co-activator, ToxS, to understand the mechanisms of ToxR transcription factor activation. ToxR is a key transcription activator that is supported by ToxS for virulence gene regulation in Vibrio cholerae. ToxR comprises a cytoplasmic DNA-binding domain that is linked by a transmembrane domain to a periplasmic signal receiver domain containing two cysteine residues. ToxR-ToxR and ToxR-ToxS PPIs were detected using an adenylate-cyclase-based bacterial two-hybrid system approach in Escherichia coli. We found that the ToxR-ToxR PPIs are significantly increased in response to ToxR operators, the co-activator ToxS and bile salts. We suggest that ToxS and bile salts promote the interaction between ToxR molecules that ultimately results in dimerization. Upon binding of operators, ToxR-ToxR PPIs are found at the highest frequency. Moreover, disulfide-bond-dependent interaction in the periplasm results in homodimer formation that is promoted by DNA binding. The formation of these homodimers and the associated transcriptional activity of ToxR were strongly dependent on the oxidoreductases DsbA/DsbC. These findings show that protein and non-protein partners, that either transiently or stably interact with ToxR, fine-tune ToxR PPIs, and its associated transcriptional activity in changing environments.
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