This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Muff, T. J.
Right arrow Articles by Ordal, G. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Muff, T. J.
Right arrow Articles by Ordal, G. W.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2007, p. 7007-7013, Vol. 189, No. 19
0021-9193/07/$08.00+0     doi:10.1128/JB.00896-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

CheX in the Three-Phosphatase System of Bacterial Chemotaxis{triangledown}

Travis J. Muff, Richard M. Foster, Peter J. Y. Liu, and George W. Ordal*

Department of Biochemistry, Colleges of Medicine and Liberal Arts and Sciences, University of Illinois, Urbana, Illinois 61801

Received 7 June 2007/ Accepted 24 July 2007

Bacterial chemotaxis involves the regulation of motility by a modified two-component signal transduction system. In Escherichia coli, CheZ is the phosphatase of the response regulator CheY but many other bacteria, including Bacillus subtilis, use members of the CheC-FliY-CheX family for this purpose. While Bacillus subtilis has only CheC and FliY, many systems also have CheX. The effect of this three-phosphatase system on chemotaxis has not been studied previously. CheX was shown to be a stronger CheY-P phosphatase than either CheC or FliY. In Bacillus subtilis, a cheC mutant strain was nearly complemented by heterologous cheX expression. CheX was shown to overcome the {Delta}cheC adaptational defect but also generally lowered the counterclockwise flagellar rotational bias. The effect on rotational bias suggests that CheX reduced the overall levels of CheY-P in the cell and did not truly replicate the adaptational effects of CheC. Thus, CheX is not functionally redundant to CheC and, as outlined in the discussion, may be more analogous to CheZ.


* Corresponding author. Mailing address: University of Illinois, 506 S Matthews, 190 MSB, Urbana, IL 61801. Phone: (217) 333-9098. Fax: (217) 333-8868. E-mail: ordal{at}uiuc.edu

{triangledown} Published ahead of print on 3 August 2007.


Journal of Bacteriology, October 2007, p. 7007-7013, Vol. 189, No. 19
0021-9193/07/$08.00+0     doi:10.1128/JB.00896-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Porter, S. L., Roberts, M. A. J., Manning, C. S., Armitage, J. P. (2008). A bifunctional kinase-phosphatase in bacterial chemotaxis. Proc. Natl. Acad. Sci. USA 105: 18531-18536 [Abstract] [Full Text]  
  • Muff, T. J., Ordal, G. W. (2007). The CheC Phosphatase Regulates Chemotactic Adaptation through CheD. J. Biol. Chem. 282: 34120-34128 [Abstract] [Full Text]