HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 15, 11562-11572, April 13, 2007

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 282/15/11562    most recent M609733200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hardwick, S. W. Articles by Lewis, R. J. Search for Related Content PubMed PubMed Citation Articles by Hardwick, S. W. Articles by Lewis, R. J. Social Bookmarking                      What's this?

Structural and Functional Characterization of Partner Switching Regulating the Environmental Stress Response in Bacillus subtilis^*

Steven W. Hardwick, Jan Pané-Farré, Olivier Delumeau, Jon Marles-Wright, James W. Murray¹, Michael Hecker, and Richard J. Lewis²

From the Institute for Cell and Molecular Biosciences, Faculty of Medical Sciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom and Institute for Microbiology, Ernst-Moritz-Arndt-University, Greifswald D-17487, Germany

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, ^B, 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."

Received for publication, October 16, 2006 , and in revised form, February 6, 2007.

The atomic coordinates and structure factors (code 2J6Y, 2J6Z, and 2J70) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the Biotechnology and Biological Sciences Research Council, the Wellcome Trust, and the University of Newcastle-upon-Tyne. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Tables 1a and 1b.

¹ Present address: Wolfson Laboratories, Dept. of Biological Sciences, Imperial College, London, London SW7 2AZ, UK.

² To whom correspondence should be addressed. Tel.: 44-191-222-5482; Fax: 44-191-222-7424; E-mail: R.Lewis{at}ncl.ac.uk.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Pane-Farre, B. Jonas, S. W. Hardwick, K. Gronau, R. J. Lewis, M. Hecker, and S. Engelmann Role of RsbU in Controlling SigB Activity in Staphylococcus aureus following Alkaline Stress J. Bacteriol., April 15, 2009; 191(8): 2561 - 2573. [Abstract] [Full Text] [PDF]

				Q. C. Truong-Bolduc, Y. Ding, and D. C. Hooper Posttranslational Modification Influences the Effects of MgrA on norA Expression in Staphylococcus aureus J. Bacteriol., November 15, 2008; 190(22): 7375 - 7381. [Abstract] [Full Text] [PDF]

				J. Marles-Wright, T. Grant, O. Delumeau, G. van Duinen, S. J. Firbank, P. J. Lewis, J. W. Murray, J. A. Newman, M. B. Quin, P. R. Race, et al. Molecular Architecture of the "Stressosome," a Signal Integration and Transduction Hub Science, October 3, 2008; 322(5898): 92 - 96. [Abstract] [Full Text] [PDF]