Team:Glasgow/PDE

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<b>The structure and function of C-Di-GMP.</b> C-Di-GMP is created by the enzyme deguanylate cyclases and is broken down by phosphodiesterases. High levels are of c-di-GMP activate functions that are necessary for biofilm growth. Image from "Principles of c-di-GMP signalling in bacteria" by  
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<b>The structure and function of C-Di-GMP.</b> C-Di-GMP is created by the enzyme deguanylate cyclases and is broken down by phosphodiesterases. High levels are of c-di-GMP activate functions that are necessary for biofilm growth. Image from "Principles of c-di-GMP signalling in bacteria" by Regine Hengge.
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Revision as of 13:03, 20 September 2011

C-Di-GMP Phosphodiesterase

Phosphodiesterases are a family of enzymes naturally present in microorganisms, which break phosphodiester bonds. The specific enzyme we are using breaks the phosphodiester bond in the second messenger nucleotide, cyclic digaunylate (cyclic-di-GMP). Cyclic-di-GMP is important in many bacterial processes, including biofilm formation and motility. The enzyme regulates signal transduction by controlling levels of the signalling molecule in cells. This approach of quenching the c-di-GMP signal has been shown to disperse biofilm.(Ma et al)

This enzyme was amplified from the genome of Pseudomonas aeruginosa PA01. The enzyme contains a domain (vieA) which specifically targets the cyclic-di-GMP molecule. We are using the enzyme to control the levels of cyclic-di-GMP within the cell. We expect that the targeted expression of phosphodesiterase could be used to interfere with biofilm formation or to trigger dispersal.

Due to the number of processes in which cyclic-di-GMP is used by prokarytes, we hope that future iGEM teams will find diverse uses for it.

The structure and function of C-Di-GMP. C-Di-GMP is created by the enzyme deguanylate cyclases and is broken down by phosphodiesterases. High levels are of c-di-GMP activate functions that are necessary for biofilm growth. Image from "Principles of c-di-GMP signalling in bacteria" by Regine Hengge.