ArticleBMC microbiology2013
Characterization of the PAS domain in the sensor-kinase BvgS: mechanical role in signal transmission.
Article in BMC microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed.
- Conformational diversity in poly-HAMP arrays and its implications for signal transduction.Protein science : a publication of the Protein Society · 2026Article
- Bordetella bronchiseptica diguanylate cyclase BdcB inhibits the type three secretion system and impacts the immune response.Scientific reports · 2023Article
- Diversity in Sensing and Signaling of Bacterial Sensor Histidine Kinases.Biomolecules · 2021Review
- Structural insight into the role of the PAS domainfor signal transduction in sensor-kinase BvgS.Journal of bacteriology · 2021Article
- The BvgS PAS Domain, an Independent Sensory Perception Module in theJournal of bacteriology · 2019Article
- A Novel Bvg-Repressed Promoter CausesJournal of bacteriology · 2018Article
- Article
- Comparison of the Whole Cell Proteome and Secretome of EpidemicFrontiers in microbiology · 2018Article
- Structural and Functional Analysis of the Escherichia coli Acid-Sensing Histidine Kinase EvgS.Journal of bacteriology · 2017Article
- Conformational Changes of an Interdomain Linker Mediate Mechanical Signal Transmission in Sensor Kinase BvgS.Journal of bacteriology · 2017Article
- Article
- Article
- Comparative genomic analysis of the swine pathogen Bordetella bronchisepticastrain KM22.Veterinary microbiology · 2016Article
- Signal Transduction by BvgS Sensor Kinase: BINDING OF MODULATOR NICOTINATE AFFECTS THE CONFORMATION AND DYNAMICS OF THE ENTIRE PERIPLASMIC MOIETY.The Journal of biological chemistry · 2015Article
- Virulence regulation with Venus flytrap domains: structure and function of the periplasmic moiety of the sensor-kinase BvgS.PLoS pathogens · 2015Article
- Characterization of mutations in the PAS domain of the EvgS sensor kinase selected by laboratory evolution for acid resistance in Escherichia coli.Molecular microbiology · 2014Article
- Evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis.PloS one · 2014Article
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6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundIn bacteria, signal-transduction two-component systems are major players for adaptation to environmental stimuli. The perception of a chemical or physical signal by a sensor-kinase triggers its autophosphorylation. The phosphoryl group is then transferred to the cognate response regulator, which mediates the appropriate adaptive response. Virulence of the whooping cough agent Bordetella pertussis is controlled by the two-component system BvgAS. Atypically, the sensor-kinase BvgS is active without specific stimuli at 37°C in laboratory conditions and is inactivated by the addition of negative chemical modulators. The structure of BvgS is complex, with two tandem periplasmic Venus flytrap domains and a cytoplasmic PAS domain that precedes the kinase domain, which is followed by additional phosphotransfer domains. PAS domains are small, ubiquitous sensing or regulatory domains. The function of the PAS domain in BvgS remains unknown.
resultsWe showed that recombinant BvgS PAS proteins form dimers that are stabilized by α helical regions flanking the PAS core. A structural model of the PAS domain dimer was built and probed by site-directed mutagenesis and by biochemical and functional analyses. Although we found no ligands for the PAS domain cavity, its integrity is required for signaling. We also showed that the structural stability of the PAS core and its proper coupling to its flanking N- and C-terminal α helices are crucial for BvgS activity.
conclusionsWe propose that a major function of the BvgS PAS domain is to maintain conformational signals arising from mechanical strain generated by the periplasmic domain. The tight structure of the PAS core and its connections with the upstream and downstream helices ensure signaling to the kinase domain, which determines BvgS activity. Many mild substitutions that map to the PAS domain keep BvgS active but make it unresponsive to negative modulators, supporting that modulation increases conformational strain in the protein.
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