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Chapter 23 : Cyclic Di-GMP: Using the Past To Peer into the Future

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Abstract:

Just over 20 years have elapsed since cyclic di-GMP (c-di-GMP) was discovered as an allosteric effector of cellulose biosynthesis. This chapter dispels myths concerning current paradigms and highlight key questions currently under investigation. Bioinformatics, and the prevalence of this molecule, provided the necessary boost to lift the study of c-di-GMP from a single laboratory to a community of researchers. Most often, these dual-domain proteins possess one highly conserved domain and one poorly conserved domain and exhibit a single activity: the one from the more well conserved domain. In some cases, enzymatically inactive domains can bind the substrate: GTP by the inactive GGDEF domain for phosphodiesterases (PDEs) and c-di-GMP by the inactive EAL domain for diguanylate cyclases (DGCs). To regulate cellular processes, c-di-GMP must be sensed. Thus, effectors must exist that bind c-di-GMP and, in response, impact some downstream target. It is widely accepted that biofilm formation is a major virulence factor for many pathogenic bacteria. Importantly, biofilm cells exhibit significantly increased resistance to antibiotics and other stresses. Beyond controlling bacterial infections, c-di-GMP may also be useful for stimulating the immune system. In most cases, the REC domain within the response regulator is linked to an effector domain. In the majority of these cases, this effector domain functions in the binding of the response regulator to DNA.

Citation: Visick K, Wolfe A. 2010. Cyclic Di-GMP: Using the Past To Peer into the Future, p 323-332. In Wolfe A, Visick K (ed), The Second Messenger Cyclic Di-GMP. ASM Press, Washington, DC. doi: 10.1128/9781555816667.ch23

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