Conformational change of the Bordetella response regulator BvgA accompanies its activation of the B. pertussis virulence gene fhaB.

ABSTRACT: The BvgAS two-component system regulates virulence gene expression in Bordetella pertussis. Although precise three-dimensional structural information is not available for the response regulator BvgA, its sequence conservation with E. coli NarL and previous studies have indicated that it is composed of 3 domains: an N-terminal domain (NTD) containing the phosphorylation site, a linker, and a DNA-binding C-terminal domain (CTD). Previous work has determined how BvgA^CTD dimers interact with the promoter (P _fhaB ) of fhaB, the gene encoding the virulence adhesin filamentous hemagglutinin. Here we use molecular modeling, FeBABE footprinting, and crosslinking to show that within the transcription complex of phosphorylated BvgA (BvgA ∼ P),

SUBMITTER: Kim D 

PROVIDER: S-EPMC9708447 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature