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A Symphony of Cyclases: Specificity in Diguanylate Cyclase Signaling

A Symphony of Cyclases: Specificity in Diguanylate Cyclase Signaling Cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. A major area of research over the last several years has been aimed at understanding how a cell with dozens of diguanylate cyclases can deploy a given subset of them to produce a desired phenotypic outcome without undesired cross talk between c-di-GMP-dependent systems. Several models have been put forward to address this question, including specificity of cyclase activation, tuned binding constants of effector proteins, and physical interaction between cyclases and effectors. Additionally, recent evidence has suggested that there may be a link between the catalytic state of a cyclase and its physical contact with an effector. This review highlights several key studies, examines the proposed global and local models of c-di-GMP signaling specificity in bacteria, and attempts to identify the most fruitful steps that can be taken to better understand how dynamic networks of sibling cyclases and effector proteins result in sensible outputs that govern cellular behavior. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Microbiology Annual Reviews

A Symphony of Cyclases: Specificity in Diguanylate Cyclase Signaling

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Publisher
Annual Reviews
Copyright
Copyright 2017 by Annual Reviews. All rights reserved
ISSN
0066-4227
eISSN
1545-3251
DOI
10.1146/annurev-micro-090816-093325
pmid
28645224
Publisher site
See Article on Publisher Site

Abstract

Cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. A major area of research over the last several years has been aimed at understanding how a cell with dozens of diguanylate cyclases can deploy a given subset of them to produce a desired phenotypic outcome without undesired cross talk between c-di-GMP-dependent systems. Several models have been put forward to address this question, including specificity of cyclase activation, tuned binding constants of effector proteins, and physical interaction between cyclases and effectors. Additionally, recent evidence has suggested that there may be a link between the catalytic state of a cyclase and its physical contact with an effector. This review highlights several key studies, examines the proposed global and local models of c-di-GMP signaling specificity in bacteria, and attempts to identify the most fruitful steps that can be taken to better understand how dynamic networks of sibling cyclases and effector proteins result in sensible outputs that govern cellular behavior.

Journal

Annual Review of MicrobiologyAnnual Reviews

Published: Sep 8, 2017

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