Logo Jena Bioscience - Building Blocks of Life

Cyclic di-GMP (c-di-GMP): A Universal Bacterial Second Messenger

c-di-GMP[1] is a pleiotropic second messenger unique to bacteria. The cellular level of c-di-GMP is tightly regulated in response to external and internal stimuli (Scheme 1)[2], and cellular c-di-GMP concentrations are directly correlated with phenotypic changes such as mobility[3], sessility[3], biofilm formation[4] and virulence[5]. To study the molecular basis of c-di-CMP signaling as well as interactions with bacterial hosts, synthetic c-di- GMP is an indispensable tool, permitting researchers to

  • quantify c-di-GMP[6]
  • understand molecular mechanisms of c-di-GMP biosynthesis[7]
  • elucidate structural basis of c-di-GMP interactions[8]
  • correlate c-di-GMP levels with phenotypes[9]
  • mimic immunogenic host response[10]

c-di-GMP and its breakdown product pGpG in stock at Jena Bioscience. For other cyclic or linear dinucleotide pairs, please inquire!

Available c-di-GMP analogs

For product information and ordering please click here:
  • cyclic-di-GMP (c-di-GMP)
  • pGpG

Scheme 1: c-di-GMP biosynthesis, breakdown and mode of action.

Scheme 1: c-di-GMP biosynthesis, breakdown and mode of action. Diguanylate cyclases (DGCs) are GGDEF-domain proteins that are activated by external or internal triggers and catalyze the synthesis of c-di-GMP from two GTP molecules. c-di-GMP exerts its functions by binding to cognate effector proteins and RNA riboswitches. Deactivation of c-di-GMP is achieved on two different pathways. Cleavage by EAL-class phosphodiesterases (PDEs) yields pGpG, while both phosphodiester bonds are hydrolyzed by HD-GYP-class PDEs, thereby generating GMP (adapted from Jenal et al.[2]).

Selected references:
[1] Ross et al. (1987) Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid. Nature 325:279.
[2] Jenal et al. (2017) Cyclic di-GMP: second messenger extraordinaire. Nat. Rev. Microbiol. 15:271.
[3] Simm (2004) GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility. Mol. Microbiol. 53:1123.
[4] Tischler et al. (2004) Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation. Mol. Microbiol. 53:857.
[5] Kulasakara et al. (2006) Analysis of Pseudomonas aeruginosa diguanylate cyclases and phosphodiesterases reveals a role for bis-(3′-5′)-cyclic-GMP in virulence. Proc. Natl. Acad. Sci. USA 103:2839.
[6] Roy et al. (2013) Extraction and Quantification of Cyclic Di-GMP from P. aeruginosa. Bio Protoc. 3:e828.
[7] Stelitano et al. (2013) Probing the activity of diguanylate cyclases and c-di-GMP phosphodiesterases in real-time by CD spectroscopy. Nucleic Acids Res. 41 (7):e79.
[8] Shang et al. (2012) Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP. Nat. Struct. Mol. Biol. 19:725.
[9] Skotnicka et al. (2016) A Minimal Threshold of c-di-GMP Is Essential for Fruiting Body Formation and Sporulation in Myxococcus xanthus. PLoS Genet. 12:e1006080.
[10] Karaolis et al. (2007) Bacterial c-di-GMP is an immunostimulatory molecule. J. Immunol. 178:2171.

Responsible for content / Imprint:
Jena Bioscience GmbH
Loebstedter Str. 71 | 07749 Jena | Germany
Phone: +49 – 3641 – 6285 000 | Fax: +49 – 3641 – 6285 100 | E-Mail: info@jenabioscience.com

Register Court:
Amtsgericht Jena, HRB 207171 | VAT No.: DE 195825742

Managing Directors: Thomas Billert | Dr. Mathias Grün

Jena Bioscience Facebook Jena Bioscience Google+ Jena Bioscience Youtube Jena Bioscience LinkedIn