World Library  
Flag as Inappropriate
Email this Article

Cyclic di-GMP

Article Id: WHEBN0017913100
Reproduction Date:

Title: Cyclic di-GMP  
Author: World Heritage Encyclopedia
Language: English
Subject: Cyclic di-GMP-I riboswitch, Deoxyribonucleoside, Ribonucleoside, Deoxycytidine monophosphate, Deoxyguanosine diphosphate
Publisher: World Heritage Encyclopedia

Cyclic di-GMP

Cyclic di-GMP
Other names
Cyclic diguanylate; 3',5'-Cyclic diguanylic acid; c-di-GMP; 5GP-5GP
ChemSpider  N
Jmol-3D images Image
Molar mass 690.09 g/mol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
 N  (: YesY/N?)

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 archaea, and has only been observed in eukaryotes in Dictyostelium.[2] The biological role of cyclic di-GMP was first uncovered when it was identified as an allosteric activator of a cellulose synthase found in Gluconacetobacter xylinus in order to produce microbial cellulose.[3]

In structure, it is a cycle 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 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.[1] In Gluconacetobacter xylinus c-di-GMP stimulates the polymerization of glucose into cellulose as a high affinity allosteric activator of the enzyme cellulose synthase.[4]Some diguanylate cyclase enzymes are allosterically inhibited by cyclic di-GMP.

Cyclic di-GMP levels regulate other processes via a number of mechanisms. The Gluconacetobacter xylinus cellulose synthase is allosterically stimulated 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. Recent structural studies of PilZ domains from two bacterial species have demonstrated that PilZ domains change conformation drastically upon binding to cyclic di-GMP.[5][6] This leads to the strong inference that conformational changes in PilZ domains allow the activity of targeted effector proteins (such as cellulose synthase) to be regulated by cyclic di-GMP. Riboswitches called the cyclic di-GMP-I riboswitch and cyclic di-GMP-II riboswitch regulate 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.

See also


  1. ^ a b
  2. ^
  3. ^
  4. ^ Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid P. Ross Nature, 1987
  5. ^
  6. ^
This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.

Copyright © World Library Foundation. All rights reserved. eBooks from Project Gutenberg are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.