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Mol Cell. 2011 Aug 19;43(4):550-60. doi: 10.1016/j.molcel.2011.07.018.

Regulatory cohesion of cell cycle and cell differentiation through interlinked phosphorylation and second messenger networks.

Author information

1
Biozentrum of the University of Basel, Klingelbergstrasse 50, CH-4054 Basel, Switzerland.

Abstract

In Caulobacter crescentus, phosphorylation of key regulators is coordinated with the second messenger cyclic di-GMP to drive cell-cycle progression and differentiation. The diguanylate cyclase PleD directs pole morphogenesis, while the c-di-GMP effector PopA initiates degradation of the replication inhibitor CtrA by the AAA+ protease ClpXP to license S phase entry. Here, we establish a direct link between PleD and PopA reliant on the phosphodiesterase PdeA and the diguanylate cyclase DgcB. PdeA antagonizes DgcB activity until the G1-S transition, when PdeA is degraded by the ClpXP protease. The unopposed DgcB activity, together with PleD activation, upshifts c-di-GMP to drive PopA-dependent CtrA degradation and S phase entry. PdeA degradation requires CpdR, a response regulator that delivers PdeA to the ClpXP protease in a phosphorylation-dependent manner. Thus, CpdR serves as a crucial link between phosphorylation pathways and c-di-GMP metabolism to mediate protein degradation events that irreversibly and coordinately drive bacterial cell-cycle progression and development.

PMID:
21855795
PMCID:
PMC3298681
DOI:
10.1016/j.molcel.2011.07.018
[Indexed for MEDLINE]
Free PMC Article

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