Regulatory cohesion of cell cycle and cell differentiation through interlinked phosphorylation and second messenger networks.
- Abel S Biozentrum of the University of Basel, Klingelbergstrasse 50, CH-4054 Basel, Switzerland.
- Chien P
- Wassmann P
- Schirmer T
- Kaever V
- Laub MT
- Baker TA
- Jenal U
- 2011-08-23
Published in:
- Molecular cell. - 2011
Bacterial Proteins
Caulobacter crescentus
Cell Cycle
Cell Polarity
Models, Biological
Phosphoric Diester Hydrolases
Phosphorylation
Second Messenger Systems
English
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.
- Language
-
- English
- Open access status
- green
- Identifiers
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- DOI 10.1016/j.molcel.2011.07.018
- PMID 21855795
- Persistent URL
- https://folia.unifr.ch/global/documents/4995
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