Document Detail


Structural and functional characterization of partner switching regulating the environmental stress response in Bacillus subtilis.
MedLine Citation:
PMID:  17303566     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The general stress response of Bacillus subtilis and close relatives provides the cell with protection from a variety of stresses. The upstream component of the environmental stress signal transduction cascade is activated by the RsbT kinase that switches binding partners from a 25 S macromolecular complex, the stressosome, to the RsbU phosphatase. Once the RsbU phosphatase is activated by interacting with RsbT, the alternative sigma factor, sigmaB, directs transcription of the general stress regulon. Previously, we demonstrated that the N-terminal domain of RsbU mediates the binding of RsbT. We now describe residues in N-RsbU that are crucial to this interaction by experimentation both in vitro and in vivo. Furthermore, crystal structures of the N-RsbU mutants provide a molecular explanation for the loss of interaction. Finally, we also characterize mutants in RsbT that affect binding to both RsbU and a simplified, binary model of the stressosome and thus identify overlapping binding surfaces on the RsbT "switch."
Authors:
Steven W Hardwick; Jan Pané-Farré; Olivier Delumeau; Jon Marles-Wright; James W Murray; Michael Hecker; Richard J Lewis
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-02-15
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  282     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2007 Apr 
Date Detail:
Created Date:  2007-04-09     Completed Date:  2007-05-31     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  11562-72     Citation Subset:  IM    
Affiliation:
Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom.
Data Bank Information
Bank Name/Acc. No.:
PDB/2J6Y;  2J6Z;  2J70
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MeSH Terms
Descriptor/Qualifier:
Bacillus subtilis / chemistry*,  genetics,  metabolism*
Bacterial Proteins / chemistry,  genetics,  metabolism
Crystallography, X-Ray
Gene Expression Regulation, Bacterial
Models, Molecular
Mutation / genetics
Phosphoric Monoester Hydrolases / chemistry,  genetics,  metabolism
Phosphorylation
Protein Binding
Protein Structure, Tertiary
Protein-Serine-Threonine Kinases / chemistry,  genetics,  metabolism
Surface Plasmon Resonance
Grant Support
ID/Acronym/Agency:
//Wellcome Trust
Chemical
Reg. No./Substance:
0/Bacterial Proteins; EC 2.7.1.-/RsbT protein, Bacillus subtilis; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 3.1.3.-/Phosphoric Monoester Hydrolases; EC 3.1.3.3/RsbU protein, Bacillus subtilis

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


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