PilZ domain proteins bind cyclic diguanylate and regulate diverse processes in Vibrio cholerae

Jason T. Pratt, Rita Tamayo, Anna D. Tischler, Andrew Camilli

Research output: Contribution to journalArticlepeer-review

127 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)12860-12870
Number of pages11
JournalJournal of Biological Chemistry
Volume282
Issue number17
DOIs
StatePublished - Apr 27 2007

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