A specificity determinant for phosphorylation in a response regulator prevents in vivo cross-talk and modification by acetyl phosphate.

ABSTRACT: Bacterial two-component systems (TCSs) sense stimuli and transduce signals intracellularly through phosphotransfer between cognate histidine kinases (HKs) and response regulators (RRs) to alter gene expression or behavioral responses. Without high phosphotransfer specificity between cognate HKs and RRs, cross-phosphorylation or cross-talk between different TCSs may occur and diminish responses to appropriate stimuli. Some mechanisms to reduce cross-talk involve HKs controlling levels of cognate RR phosphorylation. Conceivably, some RRs may have evolved HK-independent strategies to insulate themselves from cross-talk with acetyl phosphate (AcP) or other small phosphodonor metabolites. Initial steps in flagellar biosynthesis in Campylobacter jejuni stimulate phosphotransfer from the FlgS HK

SUBMITTER: Boll JM 

PROVIDER: S-EPMC3250149 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature