Split histidine kinases enable ultrasensitivity and bistability in two-component signaling networks.

ABSTRACT: Bacteria sense and respond to their environment through signaling cascades generally referred to as two-component signaling networks. These networks comprise histidine kinases and their cognate response regulators. Histidine kinases have a number of biochemical activities: ATP binding, autophosphorylation, the ability to act as a phosphodonor for their response regulators, and in many cases the ability to catalyze the hydrolytic dephosphorylation of their response regulator. Here, we explore the functional role of "split kinases" where the ATP binding and phosphotransfer activities of a conventional histidine kinase are split onto two distinct proteins that form a complex. We find that this unusual configuration can enable ultrasensitivity and bistability in the signal-response relationshi

SUBMITTER: Amin M 

PROVIDER: S-EPMC3591291 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature