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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Broad disorder and the allosteric mechanism of myosin II regulation by phosphorylation
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Broad disorder and the allosteric mechanism of myosin II regulation by phosphorylation

机译：广泛的疾病和肌球蛋白II的磷酸化调节变构机制

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摘要

Double electron electron resonance EPR methods was used to measure the effects of the allosteric modulators, phosphorylation, and ATP, on the distances and distance distributions between the two regulatory light chain of myosin (RLC). Three different states of smooth muscle myosin (SMM) were studied: monomers, the short-tailed subfragmervt heavy meromyosin, and SMM filaments. We reconstituted myosin with nine single cysteine spin-labeled RLC. For all mutants we found a broad distribution of distances that could not be explained by spin-label rotamer diversity. For SMM and heavy meromyosin, several sites showed two heterogeneous populations in the unphosphorylated samples, whereas only one was observed after phosphorylation. The data were consistent with the presence of two coexisting heterogeneous populations of structures in the unphosphorylated samples. The two populations were attributed to an on and off state by comparing data from unphosphorylated and phosphorylated samples. Models of these two states were generated using a rigid body docking approach derived from EM [Wendt T, Taylor D, Trybus KM, Taylor K (2001) Proc Natl Acad Sci USA 98:4361-4366] (PNAS, 2001, 98:4361-4366), but our data revealed a new feature of the off-state, which is heterogeneity in the orientation of the two RLC. Our average off-state structure was very similar to the Wendt model reveal a new feature of the off state, which is heterogeneity in the orientations of the two RLC. As found previously in the EM study, our on-state structure was completely different from the off-state structure. The heads are splayed out and there is even more heterogeneity in the orientations of the two RLC.
机译：双电子电子共振EPR方法用于测量变构调节剂，磷酸化和ATP对肌球蛋白（RLC）两条调节轻链之间的距离和距离分布的影响。研究了平滑肌肌球蛋白（SMM）的三种不同状态：单体，短尾亚fragermervt重肌球蛋白和SMM细丝。我们用九个单半胱氨酸自旋标记的RLC重构了肌球蛋白。对于所有突变体，我们发现距离的广泛分布无法用自旋标签旋转异构体解释。对于SMM和重度肌球蛋白，在未磷酸化的样品中有几个位点显示两个异质群体，而在磷酸化后仅观察到一个。数据与未磷酸化样品中两个共存的异质结构种群的存在相一致。通过比较未磷酸化和磷酸化样品的数据，将这两个种群归为开和关状态。使用来自EM的刚体对接方法生成这两个状态的模型[Wendt T，Taylor D，Trybus KM，Taylor K（2001）Proc Natl Acad Sci USA 98：4361-4366]（PNAS，2001，98：4361 -4366），但我们的数据显示了关闭状态的新功能，即两个RLC方向的异质性。我们的平均关闭状态结构与Wendt模型非常相似，揭示了关闭状态的新特征，即两个RLC方向上的异质性。正如之前在EM研究中发现的那样，我们的导通状态结构与截止状态结构完全不同。头部张开了，两个RLC的方向甚至存在更多的异质性。

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    Bertrand Vileno; Jean Chamoun; Hua Liang; Paul Brewer; Brian D. Haldeman; Kevin C. Facemyer; Bridget Salzameda; Likai Song; Hui-Chun Li; Christine R. Cremo; Piotr G. Fajer;

  • 作者单位

    National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, FL 32310,Department of Biology and Molecular Biophysics Institute,Florida State University, Tallahassee, FL 32306;

    National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, FL 32310,Department of Biology and Molecular Biophysics Institute,Florida State University, Tallahassee, FL 32306;

    National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, FL 32310,Department of Biology and Molecular Biophysics Institute,Florida State University, Tallahassee, FL 32306;

    Department of Biochemistry and Molecular Biology, University of Nevada School of Medicine, Reno,NV 89557;

    Department of Biochemistry and Molecular Biology, University of Nevada School of Medicine, Reno,NV 89557;

    Department of Biochemistry and Molecular Biology, University of Nevada School of Medicine, Reno,NV 89557;

    Department of Biochemistry and Molecular Biology, University of Nevada School of Medicine, Reno,NV 89557;

    National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, FL 32310,Department of Biology and Molecular Biophysics Institute,Florida State University, Tallahassee, FL 32306;

    National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, FL 32310,Department of Biochemistry, Tzu-Chi University, Hualien, 970 Taiwan;

    Department of Biochemistry and Molecular Biology, University of Nevada School of Medicine, Reno,NV 89557;

    National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, FL 32310,Department of Biology and Molecular Biophysics Institute,Florida State University, Tallahassee, FL 32306;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
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  • 关键词

    computational modeling; structural biology;

    机译：计算建模;结构生物学;

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