Phospho-signaling couples polar asymmetry and proteolysis within a membraneless microdomain in Caulobacter crescentus.

ABSTRACT: Asymmetric cell division in bacteria is achieved through cell polarization, where regulatory proteins are directed to specific cell poles. In Caulobacter crescentus, both poles contain a membraneless microdomain, established by the polar assembly hub PopZ, through most of the cell cycle, yet many PopZ clients are unipolar and transiently localized. We find that PopZ's interaction with the response regulator CpdR is controlled by phosphorylation, via the histidine kinase CckA. Phosphorylated CpdR does not interact with PopZ and is not localized to cell poles. At poles where CckA acts as a phosphatase, dephosphorylated CpdR binds directly with PopZ and subsequently recruits ClpX, substrates, and other members of a protease complex to the cell pole. We also find that co-recruitment of proteas

SUBMITTER: Ahmed YM 

PROVIDER: S-EPMC11519897 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature