Detailed analysis of c-di-GMP mediated regulation of csgD expression in Salmonella typhimurium

BMC Microbiology

Research Article

Annika Cimdins¹  Ute Römling¹  Irfan Ahmad²  Timo Beske³ 

[1] Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden;Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden;Department of Allied Health Sciences, University of Health Sciences, Lahore, Pakistan;Present Address: Department of Molecular Biology, Umeå University, Umeå, Sweden;Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden;Present Address: Department of Biology, Laboratory for Microbiology, Philipps-University Marburg, Marburg, Germany;

关键词: c-di-GMP;    CsgD;    GGDEF/EAL domain proteins;    rdar morphotype;    biofilm formation;    Salmonella typhimurium;   

DOI  :  10.1186/s12866-017-0934-5

 received in 2016-07-09, accepted in 2017-01-17,  发布年份 2017

来源: Springer

【 摘 要 】

BackgroundThe secondary messenger cyclic di-GMP promotes biofilm formation by up regulating the expression of csgD, encoding the major regulator of rdar biofilm formation in Salmonella typhimurium. The GGDEF/EAL domain proteins regulate the c-di-GMP turnover. There are twenty- two GGDEF/EAL domain proteins in the genome of S. typhimurium. In this study, we dissect the role of individual GGDEF/EAL proteins for csgD expression and rdar biofilm development.ResultsAmong twelve GGDEF domains, two proteins upregulate and among fifteen EAL domains, four proteins down regulate csgD expression. We identified two additional GGDEF proteins required to promote optimal csgD expression. With the exception of the EAL domain of STM1703, solely, diguanylate cyclase and phosphodiesterase activities are required to regulate csgD mediated rdar biofilm formation. Identification of corresponding phosphodiesterases and diguanylate cyclases interacting in the csgD regulatory network indicates various levels of regulation by c-di-GMP. The phosphodiesterase STM1703 represses transcription of csgD via a distinct promoter upstream region.ConclusionThe enzymatic activity and the protein scaffold of GGDEF/EAL domain proteins regulate csgD expression. Thereby, c-di-GMP adjusts csgD expression at multiple levels presumably using a multitude of input signals.

【 授权许可】

CC BY   
© The Author(s). 2017