Intramolecular arrangement of sensor and regulator overcomes relaxed specificity in hybrid two-component systems.

ABSTRACT: Cellular processes require specific interactions between cognate protein partners and concomitant discrimination against noncognate partners. Signal transduction by classical two-component regulatory systems typically entails an intermolecular phosphoryl transfer between a sensor kinase (SK) and a cognate response regulator (RR). Interactions between noncognate partners are rare because SK/RR pairs coevolve unique interfaces that dictate phosphotransfer specificity. Here we report that the in vitro phosphotransfer specificity is relaxed in hybrid two-component systems (HTCSs) from the human gut symbiont Bacteroides thetaiotaomicron, which harbor both the SK and RR in a single polypeptide. In contrast, phosphotransfer specificity is retained in classical two-component regulatory systems fro

SUBMITTER: Townsend GE 

PROVIDER: S-EPMC3545799 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature