Comprehensive analysis of OmpR phosphorylation, dimerization, and DNA binding supports a canonical model for activation.

ABSTRACT: The OmpR/PhoB family of response regulators (RRs) is the largest class of two-component system signal transduction proteins. Extensive biochemical and structural characterization of these transcription factors has provided insights into their activation and DNA-binding mechanisms. For the most part, OmpR/PhoB family proteins are thought to become activated through phosphorylation from their cognate histidine kinase partners, which in turn facilitates an allosteric change in the RR, enabling homodimerization and subsequently enhanced DNA binding. Incongruently, it has been suggested that OmpR, the eponymous member of this RR family, becomes activated via different mechanisms, whereby DNA binding plays a central role in facilitating dimerization and phosphorylation. Characterization of the r

SUBMITTER: Barbieri CM 

PROVIDER: S-EPMC3646996 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature