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PMID: 12237413 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

A signal transduction protein cues proteolytic events critical to Caulobacter cell cycle progression.

Hung DY, Shapiro L

Abstract

Temporally controlled proteolysis of the essential response regulator, CtrA, is critical for cell cycle progression in Caulobacter crescentus. CtrA binds to and silences the origin of replication in swarmer cells. The initiation of replication depends on the proteolysis of CtrA. We present evidence that DivK, an essential single-domain response regulator, contributes to the control of the G(1)-S transition by signaling the temporally controlled proteolysis of CtrA. In a divK-cs mutant at the restrictive temperature, the initiation of DNA replication is blocked because of the retention of CtrA. A shift of cells from restrictive to permissive temperature results in rapid degradation of CtrA, initiation of DNA replication, and the resumption of cell cycle progression, including the ordered expression of genes involved in chromosome replication and polar organelle biogenesis. CtrA binds to and regulates the promoters of two genes critical to its temporally controlled proteolysis, divK and clpP, providing a transcriptional feedback loop for the control of cell cycle progression.

MeSH Terms
Bacterial Proteins/genetics,metabolism Base Sequence Caulobacter/genetics,metabolism,physiology Cell Cycle Cell Survival DNA-Binding Proteins/genetics,metabolism Deoxyribonuclease I/metabolism Flow Cytometry Immunoblotting Models, Biological Molecular Sequence Data Mutation Oligonucleotide Array Sequence Analysis Phosphorylation Precipitin Tests Promoter Regions, Genetic Protein Binding RNA, Messenger/metabolism Replication Origin Signal Transduction Temperature Time Factors Transcription Factors/genetics,metabolism
Chemicals
Bacterial Proteins CtrA protein, Caulobacter DNA-Binding Proteins DivK protein, Caulobacter crescentus RNA, Messenger Transcription Factors Deoxyribonuclease I
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hung Dean Y
Department of Developmental Biology, Beckman Center, Stanford University School of Medicine, Stanford, CA 94305, USA.
Shapiro Lucy
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
2002-10-01
Epub
2002-00-17
Pages
13160-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC130603
Subset
IM
Grants
PHS HHS · 3206/512M2 · United States
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