PilZ Domain Proteins Bind Cyclic Diguanylate and Regulate Diverse Processes in Vibrio cholerae

Cyclic diguanylate (c-di-GMP) is an allosteric activator and second messenger implicated in the regulation of a variety of biological processes in diverse bacteria. In Vibrio cholerae, c-di-GMP has been shown to inversely regulate biofilm-specific and virulence gene expression, suggesting that c-di-...

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Bibliographic Details
Published in:The Journal of biological chemistry 2007-04, Vol.282 (17), p.12860-12870
Main Authors: Pratt, Jason T., Tamayo, Rita, Tischler, Anna D., Camilli, Andrew
Format: Article
Language:English
Subjects:
Bacterial Proteins - metabolism
Biofilms - growth & development
Cyclic GMP - analogs & derivatives
Cyclic GMP - metabolism
Protein Structure, Tertiary - physiology
Signal Transduction - physiology
Vibrio cholerae
Vibrio cholerae - growth & development
Vibrio cholerae - pathogenicity
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Summary:Cyclic diguanylate (c-di-GMP) is an allosteric activator and second messenger implicated in the regulation of a variety of biological processes in diverse bacteria. In Vibrio cholerae, c-di-GMP has been shown to inversely regulate biofilm-specific and virulence gene expression, suggesting that c-di-GMP signaling is important for the transition of V. cholerae from the environment to the host. However, the mechanism behind this regulation remains unknown. Recently, it was proposed that the PilZ protein domain represents a c-di-GMP-binding domain. Here we show that V. cholerae PilZ proteins bind c-di-GMP specifically and are involved in the regulation of biofilm formation, motility, and virulence. These findings confirm a role for PilZ proteins as c-di-GMP-sensing proteins within the c-di-GMP signaling network.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M611593200