| Coupling prokaryotic cell fate and division control with a bifunctional and oscillating oxidoreductase homolog. | |
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MedLine Citation:
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PMID: 20152180 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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NAD(H)-binding proteins play important roles in cell-cycle and developmental signaling in eukaryotes. We identified a bifunctional NAD(H)-binding regulator (KidO) that integrates cell-fate signaling with cytokinesis in the bacterium Caulobacter crescentus. KidO stimulates the DivJ kinase and directly acts on the cytokinetic tubulin, FtsZ, to tune cytokinesis with the cell cycle. At the G1-->S transition, DivJ concomitantly signals the ClpXP-dependent degradation of KidO and CtrA, a cell-cycle transcriptional regulator/DNA replication inhibitor. This proteolytic event directs KidO and CtrA into oscillatory cell-cycle abundance patterns that coordinately license replication and cytokinesis. KidO resembles NAD(P)H-dependent oxidoreductases, and conserved residues in the KidO NAD(H)-binding pocket are critical for regulation of FtsZ, but not for DivJ. Since NADPH-dependent regulation by a KidO-like oxidoreductase also occurs in humans, organisms from two domains of life exploit the enzymatic fold of an ancestral oxidoreductase potentially to coordinate cellular or developmental activities with the availability of the metabolic currency, NAD(P)H. |
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Authors:
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Sunish Kumar Radhakrishnan; Sean Pritchard; Patrick H Viollier |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Developmental cell Volume: 18 ISSN: 1878-1551 ISO Abbreviation: Dev. Cell Publication Date: 2010 Jan |
Date Detail:
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Created Date: 2010-02-15 Completed Date: 2010-03-19 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101120028 Medline TA: Dev Cell Country: United States |
Other Details:
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Languages: eng Pagination: 90-101 Citation Subset: IM |
Copyright Information:
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(c) 2010 Elsevier Inc. All rights reserved. |
Affiliation:
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Department of Molecular Biology and Microbiology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, 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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metabolism Biological Clocks / physiology* Carrier Proteins / metabolism Catalytic Domain / physiology Caulobacter crescentus / enzymology*, genetics Cell Cycle / physiology Cell Cycle Proteins / genetics, metabolism Cell Division / physiology* Cell Lineage / physiology* Cytoskeletal Proteins / metabolism NAD / metabolism Oxidation-Reduction Oxidoreductases / genetics, metabolism* Phosphotransferases / metabolism Prokaryotic Cells / enzymology Tubulin / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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SIGRR016789-01A1//PHS HHS |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Carrier Proteins; 0/Cell Cycle Proteins; 0/Cytoskeletal Proteins; 0/FtsZ protein, Bacteria; 0/Tubulin; 53-84-9/NAD; EC 1.-/Oxidoreductases; EC 2.7.-/Phosphotransferases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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