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Methods Mol Biol. 2017;1657:23-29. doi: 10.1007/978-1-4939-7240-1_3.

Synthesis of [32P]-c-di-GMP for Diguanylate Cyclase and Phosphodiesterase Activity Determinations.

Author information

1
Department of Medicine, Yale University, 333 Cedar St., New Haven, CT, 06520-8022, USA. barbara.kazmierczak@yale.edu.
2
Department of Microbial Pathogenesis, Yale University, 333 Cedar St., New Haven, CT, 06520-8022, USA. barbara.kazmierczak@yale.edu.

Abstract

Diguanylate cyclases that synthesize and phosphodiesterases that hydrolyze the second messenger cyclic-di-GMP (c-di-GMP) are at the center of bacterial signaling pathways that control behaviors relevant to all aspects of microbial physiology and pathogenesis (Romling et al., Microbiol Mol Biol Rev 77(1):1-52, 2013). Bioinformatics tools can easily predict the presence of the diguanylate cyclase GGDEF domain, or the EAL and HD-GYP domains associated with phosphodiesterase activity. However, experimental confirmation of enzymatic activity is still necessary, as many proteins contain degenerate domains that lack catalytic activity but nonetheless function as c-di-GMP receptors.

KEYWORDS:

Cyclic-di-GMP; Diguanylate cyclase; Phosphodiesterase

PMID:
28889283
DOI:
10.1007/978-1-4939-7240-1_3
[Indexed for MEDLINE]

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