| 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 |
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| 引用本文： | 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. DOI: 10.11938/cjmr20172572 |
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| 作者姓名： | 王丹 刘乙祥 寇新慧 刘买利 姜凌 |
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| 作者单位： | 1. 中国科学院生物磁共振分析重点实验室, 波谱与原子分子物理国家重点实验室, 武汉磁共振中心(中国科学院 武汉物理与数学研究所), 湖北 武汉 430071;2. 中国科学院大学, 北京 100049 |
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| 基金项目： | 国家自然科学基金资助项目 |
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| 摘 要： | 反应调节蛋白是细菌双组分信号转导系统的重要组分，用于传递来自组氨酸激酶的信号并产生适应性反应.在整个信号转导过程中，反应调节蛋白的磷酸化和去磷酸化最终决定了该系统的信号输出和信号转导终止，因此其磷酸化和去磷酸化作用位点是控制其功能的关键要素．我们以来源于Thermotoga maritima中的反应调节蛋白RR468作为研究对象，将其分别位于loop b3-a3和loop b4-a4上的两个关键位点M55和K85进行突变，通过功能实验验证了这两个残基突变会对蛋白磷酸化和去磷酸化产生影响，并且利用液体核磁共振（NMR）手段对两个突变体的结构和动力学性质进行了研究．
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| 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 |
| 收稿时间： | 2017-04-05 |
NMR Studies on Key Residues That Affect Phosphorylation and Dephosphorylation Processes of Bacterial Response Regulator RR468 |
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| 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. DOI: 10.11938/cjmr20172572 |
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| Authors: | WANG Dan LIU Yi-xiang KOU Xin-hui LIU Mai-li JIANG Ling |
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| Affiliation: | 1. CAS Key Laboratory of Magnetic Resonance in Biological System, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, National Center for Magnetic Resonance in Wuhan(Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences), Wuhan 430071, China;2. University of Chinese Academy of Sciences, Beijing 100049, China |
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| 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. |
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| Keywords: | NMR phosphorylation protein dynamics response regulator two-component signal transduction system |
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