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 Martinez-Wilson, H. F.
Right arrow Articles by Camilli, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Martinez-Wilson, H. F.
Right arrow Articles by Camilli, A.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2008, p. 6439-6447, Vol. 190, No. 19
0021-9193/08/$08.00+0     doi:10.1128/JB.00541-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

The Vibrio cholerae Hybrid Sensor Kinase VieS Contributes to Motility and Biofilm Regulation by Altering the Cyclic Diguanylate Level {triangledown}

Hector F. Martinez-Wilson,1 Rita Tamayo,1 Anna D. Tischler,2 David W. Lazinski,1 and Andrew Camilli1*

Howard Hughes Medical Institute and the Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111,1 Global Health Institute in the School of Life Sciences at the École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland2

Received 20 April 2008/ Accepted 28 July 2008

Phosphorelay systems are important mediators of signal transduction during bacterial adaptation to new environments. Previously we described the vieSAB operon, encoding a putative three-protein component phosphorelay involved in regulating Vibrio cholerae virulence gene expression. At least part of the regulatory activity of VieSAB is exerted through the cyclic diguanylate (c-di-GMP)-degrading activity of the putative response regulator VieA. So far no direct evidence that VieSAB encodes a phosphorelay system exists. In addition, the role VieS plays in modulating VieA activity remains unclear. To address these questions, we expressed and purified VieA and a soluble cytoplasmic portion of VieS and used them in autophosphorylation and phosphotransfer assays. These assays showed that VieS has kinase activity in vitro and is able to selectively phosphorylate VieA. A phenotypic comparison revealed that deletion of vieS results in increased biofilm production comparable to that seen for deletion of vieA, whereas motility was decreased only slightly in the {Delta}vieS mutant compared to the profound defect observed in a {Delta}vieA mutant. We also found that the {Delta}vieS strain has a lower level of vieA transcript and, similar to a {Delta}vieA mutant, an increased intracellular level of c-di-GMP. Further analysis using site-directed vieA mutants showed that some of the phenotypes observed were due to the phosphorylation status of VieA. The evidence presented in this report is the first to link VieS and VieA biochemically and genetically, lending support to the hypothesis that these proteins function together in a signaling system.

* Corresponding author. Mailing address: Tufts University School of Medicine, Department of Molecular Biology and Microbiology, Boston, MA 02111. Phone: (617) 636-2144. Fax: (617) 636-2175. E-mail: andrew.camilli{at}tufts.edu

{triangledown} Published ahead of print on 1 August 2008.

Journal of Bacteriology, October 2008, p. 6439-6447, Vol. 190, No. 19
0021-9193/08/$08.00+0     doi:10.1128/JB.00541-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Hammer, B. K., Bassler, B. L. (2009). Distinct Sensory Pathways in Vibrio cholerae El Tor and Classical Biotypes Modulate Cyclic Dimeric GMP Levels To Control Biofilm Formation. J. Bacteriol. 191: 169-177 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»