Functional analysis of GGDEF-EAL didomain-containing proteins in cyclic-di-GMP signaling

Abstract

Cylic-di-GMP (c-di-GMP) is a ubiquitous bacterial second messenger that regulates twitching motility, virulence secretion, cell surface adhesion and biofilm formation. The intracellular concentrations of c-di-GMP are regulated by various GGDEF/EAL domain-containing proteins. My PhD study utilized biochemical and biophysical approaches to probe the function and mechanism of three representative GGDEF-EAL didomain-containing proteins, including PA2567, FimX from Pseudomonas aeruginosa and AxDGC2 from Acetobacter xylinum. The detailed elucidation of catalytic and regulatory mechanism of the three proteins yielded insights into the molecular mechanism of the c-di-GMP signaling network.