NMR Studies on Key Residues That Affect Phosphorylation and Dephosphorylation Processes of Bacterial Response Regulator RR468

doi:10.11938/cjmr20172572

Abstract

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 b3-a3 and loop b4-a4, 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.

Key words: NMR, phosphorylation, protein dynamics, response regulator, two-component signal transduction system

CLC Number:

O482.53

WANG Dan, LIU Yi-xiang, KOU Xin-hui, LIU Mai-li, JIANG Ling. NMR Studies on Key Residues That Affect Phosphorylation and Dephosphorylation Processes of Bacterial Response Regulator RR468[J]. Chinese Journal of Magnetic Resonance, 2017, 34(4): 397-407.

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