波谱学杂志2017，Vol.34Issue(4)：397-407,11.DOI:10.11938/cjmr20172572
细菌反应调节蛋白RR468磷酸化和去磷酸化关键位点的NMR研究
NMR Studies on Key Residues That Affect Phosphorylation and Dephosphorylation Processes of Bacterial Response Regulator RR468
摘要
Abstract
Response regulator proteins are important components of the two-component signal transduction systems, and essential in transferring the signal delivered from the sensor histidine kinase and eliciting an adaptive response. Phosphorylation and dephosphorylation of the response regulator proteins determine the direction of the signal transduction process. The phosphorylation and dephosphorylation sites of the response regulator proteins play an important role in exerting their function. Here we studied some key residues of response regulator RR468 from Thermotoga maritima. Site-directed mutagenesis experiments were performed to the key sites M55 and K85, which are located in loop β3-α3 and loop β4-α4, respectively. The structure and dynamics feature of the two mutants were investigated with liquid nuclear magnetic resonance (NMR) spectroscopy. The results of functional experiments demonstrated that the two residues could affect the phosphorylation and dephosphorylation processes.关键词
核磁共振(NMR)/磷酸化/蛋白质动力学/反应调节蛋白/双组分信号转导系统Key words
NMR/phosphorylation/protein dynamics/response regulator/two-component signal transduction system分类
数理科学引用本文复制引用
王丹,刘乙祥,寇新慧,刘买利,姜凌..细菌反应调节蛋白RR468磷酸化和去磷酸化关键位点的NMR研究[J].波谱学杂志,2017,34(4):397-407,11.基金项目
国家自然科学基金资助项目(21573280, 21603268). （21573280, 21603268）
