Progress in research on bacterial HD-GYP domain proteins / 中华微生物学和免疫学杂志
Chinese Journal of Microbiology and Immunology
; (12): 230-234, 2017.
Article
en Zh
| WPRIM
| ID: wpr-673077
Biblioteca responsable:
WPRO
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.
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1
Base de datos:
WPRIM
Idioma:
Zh
Revista:
Chinese Journal of Microbiology and Immunology
Año:
2017
Tipo del documento:
Article