| A dynamically localized protease complex and a polar specificity factor control a cell cycle master regulator. | |
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MedLine Citation:
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PMID: 16469700 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Regulated proteolysis is essential for cell cycle progression in both prokaryotes and eukaryotes. We show here that the ClpXP protease, responsible for the degradation of multiple bacterial proteins, is dynamically localized to specific cellular positions in Caulobacter where it degrades colocalized proteins. The CtrA cell cycle master regulator, that must be cleared from the Caulobacter cell to allow the initiation of chromosome replication, interacts with the ClpXP protease at the cell pole where it is degraded. We have identified a novel, conserved protein, RcdA, that forms a complex with CtrA and ClpX in the cell. RcdA is required for CtrA polar localization and degradation by ClpXP. The localization pattern of RcdA is coincident with and dependent upon ClpX localization. Thus, a dynamically localized ClpXP proteolysis complex in concert with a cytoplasmic factor provides temporal and spatial specificity to protein degradation during a bacterial cell cycle. |
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Authors:
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Patrick T McGrath; Antonio A Iniesta; Kathleen R Ryan; Lucy Shapiro; Harley H McAdams |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Cell Volume: 124 ISSN: 0092-8674 ISO Abbreviation: Cell Publication Date: 2006 Feb |
Date Detail:
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Created Date: 2006-02-10 Completed Date: 2006-03-20 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0413066 Medline TA: Cell Country: United States |
Other Details:
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Languages: eng Pagination: 535-47 Citation Subset: IM |
Affiliation:
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Department of Physics, Stanford University, Stanford, CA 94305, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Proteins
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chemistry,
genetics,
metabolism* Caulobacter / cytology*, genetics, metabolism* Cell Cycle / genetics, physiology Cell Polarity DNA-Binding Proteins / chemistry, genetics, metabolism* Endopeptidase Clp / chemistry, genetics, metabolism* Genes, Bacterial Multiprotein Complexes Recombinant Fusion Proteins / chemistry, genetics, metabolism Transcription Factors / chemistry, genetics, metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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GM32506/GM/NIGMS NIH HHS; T32 HG00044/HG/NHGRI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/CtrA protein, Caulobacter; 0/DNA-Binding Proteins; 0/Multiprotein Complexes; 0/Recombinant Fusion Proteins; 0/Transcription Factors; EC 3.4.21.92/Endopeptidase Clp |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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