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Cyclic di-GMP
Cyclic-di-gmp wiki jypx3 091210.png
Other names Cyclic diguanylate; 3',5'-Cyclic diguanylic acid; c-di-GMP; 5GP-5GP
Identifiers
CAS number 61093-23-0
PubChem 6323195
SMILES
Properties
Molecular formula C20H24N10O14P2
Molar mass 690.09 g/mol
Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
Infobox references

Cyclic di-GMP (also called cyclic diguanylate and c-di-GMP) is a second messenger used in signal transduction in a wide variety of bacteria.[1] Cyclic di-GMP is not known to be used by eukaryotes or archaea. The biological role of cyclic di-GMP was first uncovered when it was identified as an allosteric activator of a cellulose synthase found in in Gluconacetobacter xylinus.[2]

In structure, it is a tiny cycle of RNA, containing only two guanine bases linked by ribose and phosphate.

In bacteria, certain signals are communicated by synthesizing or degrading cyclic di-GMP. Cyclic di-GMP is synthesized by proteins with diguanylate cyclase activity. These proteins typically have a characteristic GGDEF motif, which refers to a conserved sequence of five amino acids. Degradation of cyclic di-GMP is effected by proteins with phosphodiesterase activity. These proteins have either an EAL or an HD-GYP amino acid motif. Processes that are known to be regulated using cyclic di-GMP, at least in some organisms, include biofilm formation, motility and induction of virulence factors.

Cyclic di-GMP levels are regulated using a variety of mechanisms. Many proteins with GGDEF, EAL or HD-GYP domains are found with other domains that can receive signals, such as PAS domains. Enzymes that degrade or synthesize cyclic di-GMP are believed to be localized to specific regions of the cell, where they influence receivers in a restricted space. Some diguanylate cyclase enzymes and a cellulose synthase in Gluconacetobacter xylinus are allosterically inhibited by cyclic di-GMP.

Cyclic di-GMP levels regulate other processes via a number of mechanisms. The Gluconacetobacter xylinus cellolose synthase is allosterically inhibited by cyclic di-GMP, presenting a mechanism by which cyclic di-GMP can regulate cellulose synthase activity. The PilZ domain has been shown to bind cyclic di-GMP and is believed to be involved in cyclic di-GMP-dependent regulation, but the mechanism by which it does this is unknown. A riboswitch called the cyclic di-GMP riboswitch has been found that regulates gene expression in response to cyclic di-GMP concentrations in a variety of bacteria, but not all bacteria that are known to use cyclic di-GMP.

References

  1. ^ Tamayo R, Pratt JT, Camilli A (2007). "Roles of cyclic diguanylate in the regulation of bacterial pathogenesis". Annu. Rev. Microbiol. 61: 131–48. doi:10.1146/annurev.micro.61.080706.093426. PMID 17480182.  
  2. ^ P. Ross, H. Weinhouse, Y. Aloni, D. Michaeli, P. Weinberger-Ohana, R. Mayer, S. Braun, E. de Vroom, G. A. van der Mare, J. H. van Boom & M. Benziman (1987). "Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid". Nature 325: 279–81. doi:10.1038/325279a0.  
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