Document Detail


Polar localization and compartmentalization of ClpP proteases during growth and sporulation in Bacillus subtilis.
MedLine Citation:
PMID:  18689476     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Spatial control of proteolysis is emerging as a common feature of regulatory networks in bacteria. In the spore-forming bacterium Bacillus subtilis, the peptidase ClpP can associate with any of three ATPases: ClpC, ClpE, and ClpX. Here, we report that ClpCP, ClpEP, and ClpXP localize in foci often near the poles of growing cells and that ClpP and the ATPase are each capable of polar localization independently of the other component. A region of ClpC containing an AAA domain was necessary and sufficient for polar localization. We also report that ClpCP and ClpXP proteases differentially localize to the forespore and mother cell compartments of the sporangium during spore formation. Moreover, model substrates for each protease created by appending recognition sequences for ClpCP or ClpXP to the green fluorescent protein were preferentially eliminated from the forespore or the mother cell, respectively. Biased accumulation of ClpCP in the forespore may contribute to the cell-specific activation of the transcription factor sigma(F) by preferential ClpCP-dependent degradation of the anti-sigma(F) factor SpoIIAB.
Authors:
James Kain; Gina G He; Richard Losick
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2008-08-08
Journal Detail:
Title:  Journal of bacteriology     Volume:  190     ISSN:  1098-5530     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2008 Oct 
Date Detail:
Created Date:  2008-10-01     Completed Date:  2008-10-28     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6749-57     Citation Subset:  IM    
Affiliation:
Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Ave., Cambridge, MA 02138, USA.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / analysis
Bacillus subtilis / enzymology*
Bacterial Proteins / analysis
Cytosol / chemistry
Endopeptidase Clp / analysis*
Genes, Reporter
Green Fluorescent Proteins / genetics,  metabolism
Heat-Shock Proteins / analysis
Prokaryotic Cells / chemistry*
Protein Structure, Tertiary
Recombinant Fusion Proteins / genetics,  metabolism
Spores, Bacterial / chemistry
Grant Support
ID/Acronym/Agency:
GM 18568/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/ClpC protein, Bacteria; 0/Heat-Shock Proteins; 0/Recombinant Fusion Proteins; 0/enhanced green fluorescent protein; 147336-22-9/Green Fluorescent Proteins; EC 3.4.21.92/Endopeptidase Clp; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/ClpE protein, bacteria
Comments/Corrections

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


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