| Mutations that alter RcdA surface residues decouple protein localization and CtrA proteolysis in Caulobacter crescentus. | |
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MedLine Citation:
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PMID: 19747489 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Periodic activation and deactivation of the essential transcriptional regulator CtrA is necessary to drive cell cycle progression in Caulobacter crescentus. At the onset of DNA replication (the G1-S cell cycle transition), CtrA and the AAA+ protease ClpXP colocalize at one cell pole along with three accessory proteins, RcdA, CpdR, and PopA, and CtrA is rapidly degraded. RcdA is required for polar sequestration and regulated proteolysis of CtrA in vivo, but it does not stimulate CtrA degradation by ClpXP in vitro; thus, the function of RcdA is unknown. We determined the 2.9-A-resolution crystal structure of RcdA and generated structure-guided mutations in rcdA. We assayed the ability of each RcdA variant to support CtrA proteolysis and polar protein localization in Caulobacter. Deletion of an intrinsically disordered peptide at the C-terminus of RcdA prevents efficient CtrA degradation and blocks the transient localization of RcdA and CtrA at the cell pole. Surprisingly, substitutions in two groups of highly conserved, charged surface residues disrupt polar RcdA or CtrA localization but do not affect CtrA proteolysis. This is the first report showing that localization of RcdA can be decoupled from its effects on CtrA degradation. In addition, we used epistasis experiments to show that RcdA is still required for regulated CtrA proteolysis when all SsrA-tagged proteins, abundant substrates of ClpXP, are absent from the cell. Our results argue that RcdA stimulates CtrA proteolysis neither by localizing CtrA at the cell pole nor by preventing competition from SsrA-tagged substrates. |
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Authors:
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James A Taylor; Jeremy D Wilbur; Stephen C Smith; Kathleen R Ryan |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. Date: 2009-09-08 |
Journal Detail:
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Title: Journal of molecular biology Volume: 394 ISSN: 1089-8638 ISO Abbreviation: J. Mol. Biol. Publication Date: 2009 Nov |
Date Detail:
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Created Date: 2009-10-27 Completed Date: 2009-11-10 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 2985088R Medline TA: J Mol Biol Country: England |
Other Details:
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Languages: eng Pagination: 46-60 Citation Subset: IM |
Affiliation:
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Department of Plant and Microbial Biology, 251 Koshland Hall, University of California, Berkeley, Berkeley, CA 94720-3102, USA. |
| Data Bank Information | |
Bank Name/Acc. No.:
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PDB/3CTW |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids
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genetics* Bacterial Proteins / chemistry*, metabolism* Caulobacter crescentus / cytology, metabolism* Cell Polarity Crystallography, X-Ray DNA-Binding Proteins / metabolism* G1 Phase Half-Life Mutant Proteins / chemistry, metabolism Mutation / genetics* Protein Binding Protein Multimerization Protein Processing, Post-Translational* Protein Structure, Secondary Protein Transport S Phase Sequence Deletion Structure-Activity Relationship Surface Properties Transcription Factors / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Bacterial Proteins; 0/CtrA protein, Caulobacter; 0/DNA-Binding Proteins; 0/Mutant Proteins; 0/Transcription Factors |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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