Chapter title |
Synthesis of [(32)P]-c-di-GMP for Diguanylate Cyclase and Phosphodiesterase Activity Determinations.
|
---|---|
Chapter number | 3 |
Book title |
c-di-GMP Signaling
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-7240-1_3 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7239-5, 978-1-4939-7240-1
|
Authors |
Kazmierczak, Barbara I, Barbara I. Kazmierczak |
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. |
X Demographics
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 2 | 100% |
Demographic breakdown
Type | Count | As % |
---|---|---|
Members of the public | 2 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 2 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 1 | 50% |
Unknown | 1 | 50% |
Readers by discipline | Count | As % |
---|---|---|
Unknown | 2 | 100% |