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• W2189859357 startingPage "37" @default.
• W2189859357 abstract "This chapter describes the studies that resulted in the experimental verification of the core signaling pathway. It discusses advances in enzymology of c-di-GMP synthesis and hydrolysis, identification and characterization of cyclic di-GMP (c-di-GMP) receptors, end targets, and molecular mechanisms, where these are known. The first line of experimental evidence that supported the prediction that DGC activity resides in the GGDEF domain came from genetic studies. If GGDEF domains were to function as diguanylate cyclase (DGC), the predicted activity of the EAL domains would have to be c-di-GMP hydrolysis. However, it was unclear whether or not EAL domains are sufficient for phosphodiesterase (PDE) activity, or whether GGDEF domains are needed as well. Spatiotemporal and stimulus-specific regulation proved to be crucial for maintaining specificity of responses and avoiding unwanted cross talk in the bacteria that possess vast networks of DGCs and PDEs. Since functional DGCs are present in representatives from various branches of the phylogenetic tree of the Bacteria, including branches comprised mostly of thermophiles, one can predict that c-di-GMP originated early in bacterial evolution. In vitro studies characterizing c-di-GMP-specific PDE activity were performed on the EAL domain proteins from other sources, Caulobacter crescentus CC3396 and Vibrio cholerae VieA, and very similar conclusions regarding the nature of enzymatic activity were reached." @default.
• W2189859357 created "2016-06-24" @default.
• W2189859357 creator A5075399498 @default.
• W2189859357 date "2014-04-30" @default.
• W2189859357 modified "2023-09-23" @default.
• W2189859357 title "The Core Pathway: Diguanylate Cyclases, Cyclic Di-GMP-Specific Phosphodiesterases, and Cyclic Di-GMP-Binding Proteins" @default.
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