Membrane association of SadC enhances its diguanylate cyclase activity to control exopolysaccharides synthesis and biofilm formation in Pseudomonas aeruginosa
(0) Cyclic diguanosine monophosphate (c-di-GMP) is one of the most important bacterial second messengers that controls many bacterial cellular functions including lifestyle switch between plankton and biofilm.Surface attachment defective (SadC) is a diguanylate cyclase (DGC) involved in the biosynthesis of c-di-GMP in Pseudomonas aeruginosa, an opportunistic pathogen that can cause diverse infections.Here we report the crystal structure of GGDEF domain from SadC and the critical role of the transmembrane (TM) domain of SadC with regard to biofilm formation, exopolyseccharide production and motility.We showed that over-expression of SadC in P.aeruginosa PAO1 totally inhibited swimming motility and significantly enhanced the production of exopolysaccharide Psl.SadC lacking TM domains (SadC300-487) could not localize on cytoplasmic membrane and form cluster, lost the ability to inhibit the swimming and twitching motility, and showed the attenuated activity to promote Psl production despite that SadC300-487 was able to catalyze the synthesize of c-di-GMP in vitro and in vivo.The GGDEF domain of SadC has a typical GGDEF structure and the α-helix connected the TM domains with SadC GGDEF domain is essential for SadC to form DGC oligomers.Our data imply that membrane association of SadC promotes its DGC activity by affecting the formation of active DGC oligomers.
Bin Zhu Cuilan Liu Shiheng Liu Hengjiang Cong Yihuan Chen Lichuan Gu Luyan Z.Ma
State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, State Key Laboratory of Microbial Technology, School of Life Sciences, Shandong University, Jinan, S State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences,
国际会议
北京
英文
528-540
2018-03-29（万方平台首次上网日期，不代表论文的发表时间）