Document Detail


Elevated ATPase activity of KaiC applies a circadian checkpoint on cell division in Synechococcus elongatus.
MedLine Citation:
PMID:  20178745     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A circadian clock coordinates physiology and behavior in diverse groups of living organisms. Another major cyclic cellular event, the cell cycle, is regulated by the circadian clock in the few cases where linkage of these cycles has been studied. In the cyanobacterium Synechococcus elongatus, the circadian clock gates cell division by an unknown mechanism. Using timelapse microscopy, we confirm the gating of cell division in the wild-type and demonstrate the regulation of cytokinesis by key clock components. Specifically, a state of the oscillator protein KaiC that is associated with elevated ATPase activity closes the gate by acting through a known clock output pathway to inhibit FtsZ ring formation at the division site. An activity that stimulates KaiC phosphorylation independently of the KaiA protein was also uncovered. We propose a model that separates the functions of KaiC ATPase and phosphorylation in cell division gating and other circadian behaviors.
Authors:
Guogang Dong; Qiong Yang; Qiang Wang; Yong-Ick Kim; Thammajun L Wood; Katherine W Osteryoung; Alexander van Oudenaarden; Susan S Golden
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Publication Detail:
Type:  Journal Article; Research Support, American Recovery and Reinvestment Act; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  Cell     Volume:  140     ISSN:  1097-4172     ISO Abbreviation:  Cell     Publication Date:  2010 Feb 
Date Detail:
Created Date:  2010-02-24     Completed Date:  2010-03-23     Revised Date:  2011-07-22    
Medline Journal Info:
Nlm Unique ID:  0413066     Medline TA:  Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  529-39     Citation Subset:  IM    
Copyright Information:
2010 Elsevier Inc. All rights reserved.
Affiliation:
Center for Biological Clocks Research, Department of Biology, Texas A&M University, College Station, 77843-3258, USA.
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MeSH Terms
Descriptor/Qualifier:
Bacterial Proteins / metabolism*
Biological Clocks
Cell Division*
Circadian Rhythm*
Circadian Rhythm Signaling Peptides and Proteins / metabolism*
Cytoskeletal Proteins / metabolism
Gene Expression Regulation, Bacterial
Phosphorylation
Protein Kinases / metabolism
Synechococcus / cytology*,  physiology*
Grant Support
ID/Acronym/Agency:
P01 NS039546-06A10005/NS/NINDS NIH HHS; P01 NS39546/NS/NINDS NIH HHS; R01 GM062419-05A2/GM/NIGMS NIH HHS; R01 GM062419-06/GM/NIGMS NIH HHS; R01 GM062419-07/GM/NIGMS NIH HHS; R01 GM062419-07S1/GM/NIGMS NIH HHS; R01 GM062419-10/GM/NIGMS NIH HHS; R01 GM068957/GM/NIGMS NIH HHS; R01 GM62419/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Circadian Rhythm Signaling Peptides and Proteins; 0/Cytoskeletal Proteins; 0/FtsZ protein, Bacteria; 0/KaiC protein, cyanobacteria; EC 2.7.-/Protein Kinases; EC 2.7.3.-/CikA protein, bacteria
Comments/Corrections
Comment In:
Cell. 2010 Feb 19;140(4):458-9   [PMID:  20178739 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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