Progress in research on bacterial HD-GYP domain proteins
10.3760/cma.j.issn.0254-5101.2017.03.012
- VernacularTitle:细菌HD-GYP结构域蛋白研究进展
- Author:
Liangliang KONG
;
Jie YAN
;
Xu′ai LIN
;
- Keywords:
Cyclic diguanylate;
Phosphodiesterase;
HD-GYP domain
- From:
Chinese Journal of Microbiology and Immunology
2017;37(3):230-234
- CountryChina
- Language:Chinese
-
Abstract:
Bis-(3′,5′) cyclic di-guanylate (c-di-GMP) is an almost ubiquitous intracellular second messenger in bacteria.Now it is known to regulate complex physiological processes, including mobility, adhesion, virulence and biofilm formation.The level of c-di-GMP is regulated by diguanylate cyclases (DGCs) containing GGDEF domains and phosphodiesterases (PDEs) containing EAL or HD-GYP domains.Recent studies have demonstrated that HD-GYP domain protein is a novel phosphodiesterase, which is also involved in the regulation of c-di-GMP degradation.This review highlights recent advances in the structure and biochemical functions of HD-GYP domain proteins, which might help to further clarify the mechanism of c-di-GMP signal system.
