例如:"lncRNA", "apoptosis", "WRKY"

The REC domain mediated dimerization is critical for FleQ from Pseudomonas aeruginosa to function as a c-di-GMP receptor and flagella gene regulator.

J. Struct. Biol.2015 Oct;192(1):1-13. Epub 2015 Sep 08
Tiantian Su 1 , Shiheng Liu 1 , Kang Wang 1 , Kaikai Chi 1 , Deyu Zhu 1 , Tiandi Wei 1 , Yan Huang 1 , Liming Guo 2 , Wei Hu 1 , Sujuan Xu 1 , Zong Lin 3 , Lichuan Gu 4
Tiantian Su 1 , Shiheng Liu 1 , Kang Wang 1 , Kaikai Chi 1 , Deyu Zhu 1 , Tiandi Wei 1 , Yan Huang 1 , Liming Guo 2 , Wei Hu 1 , Sujuan Xu 1 , Zong Lin 3 , Lichuan Gu 4
+ et al

[No authors listed]

Author information
  • 1 State Key Laboratory of Microbial Technology, School of Life Sciences, Shandong University, Jinan 250100, Shandong, China.
  • 2 Rizhao Center for Diseases Prevention and Control, Rizhao Health Bureau, Rizhao 276826, Shandong, China.
  • 3 Department of Biotechnology and Biomedicine, Yangtze Delta Region Institute of Tsinghua University, Jiaxing, Zhejiang 314006, China.
  • 4 State Key Laboratory of Microbial Technology, School of Life Sciences, Shandong University, Jinan 250100, Shandong, China. Electronic address: lcgu@sdu.edu.cn.

摘要


FleQ is an AAA+ ATPase enhancer-binding protein that regulates both flagella and biofilm formation in the opportunistic pathogen Pseudomonas aeruginosa. FleQ belongs to the NtrC subfamily of response regulators, but lacks the corresponding aspartic acid for phosphorylation in the REC domain (FleQ(R), also named FleQ domain). Here, we show that the atypical REC domain of FleQ is essential for the function of FleQ. Crystal structure of FleQ(R) at 2.3Å reveals that the structure of FleQ(R) is significantly different from the REC domain of NtrC1 which regulates gene expression in a phosphorylation dependent manner. FleQ(R) forms a novel active dimer (transverse dimer), and mediates the dimerization of full-length FleQ in an unusual manner. Point mutations that affect the dimerization of FleQ lead to loss of function of the protein. Moreover, a c-di-GMP binding site deviating from the previous reported one is identified through structure analysis and point mutations.

KEYWORDS: Biofilm, Cyclic di-GMP, Flagella, Pseudomonas aeruginosa, Structure–function, Transcription factor