Journal
MOLECULAR CELL
Volume 38, Issue 1, Pages 128-139Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2010.03.001
Keywords
-
Categories
Funding
- Welch foundation [F-1351]
- U.S. National Institutes of Health (NIH) [R01GM64664, GM57400]
- Dale A. Stringfellow Graduate Fellowship in Microbiology
Ask authors/readers for more resources
We describe a mechanism of flagellar motor control by the bacterial signaling molecule c-di-GMP, which regulates several cellular behaviors. E. coli and Salmonella have multiple c-di-GMP cyclases and phosphodiesterases, yet absence of a specific phosphodiesterase YhjH impairs motility in both bacteria. yhjH mutants have elevated c-di-GMP levels and require YcgR, a c-di-GMP-binding protein, for motility inhibition. We demonstrate that YcgR interacts with the flagellar switch-complex proteins FliG and FliM, most strongly in the presence of c-di-GMP. This interaction reduces the efficiency of torque generation and induces CCW motor bias. We present a backstop brake model showing how both effects can result from disrupting the organization of the FliG C-terminal domain, which interacts with the stator protein MotA to generate torque. Inhibition of motility and chemotaxis may represent a strategy to prepare for sedentary existence by disfavoring migration away from a substrate on which a biofilm is to be formed.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available