Characterization of the PAS domain in the sensor-kinase BvgS: mechanical role in signal transmission.

ABSTRACT:

Background

In 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 follow

SUBMITTER: Dupre E 

PROVIDER: S-EPMC3726324 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature