| Abstrakt: |
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 protease components and substrates to polar microdomains enhances their coordinated activity. This study connects phospho-signaling with polar assembly and the activity of a protease that triggers cell cycle progression and cell differentiation. Asymmetric bacterial cell division involves the polar organizing protein PopZ recruiting cell fate regulators. Here, the authors show that, in Caulobacter crescentus, phosphorylation directly regulates client protein interactions with the PopZ hub. [ABSTRACT FROM AUTHOR] |
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