Role of the unique loops located in the dotor domain of myosin and kinesin

位于肌球蛋白和驱动蛋白 dotor 结构域的独特环的作用

• 批准号: 11680667
• 负责人: MARUTA Shinsaku
• 金额: $ 1.66万
• 依托单位: Soka University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 1999
• 资助国家: 日本
• 起止时间: 1999 至 2001
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-11680667/
• 关键词: Molecular motor; Myosin; Kinesin; Loop; Transition state analog; Mutant; Fluorescence; Conformational change; ATPアナログ; ^<19>F-NMR

The structure of the motor domains of myosin and kinesin are highly conserved. Thus, these motor proteins may share a common mechanism for generating energy for from ATP hydrolysis. Nevertheless, myosin and kinesin have several unique loops in each motor domain. The precise function of the loops is as yet known, but they may have roles in determining the characteristic properties of each motor protein. In the present study, the conformational changes of the loops in ATPase were studied using several biochemical and molecular biological techniques and the experimental results suggested that the loops might act as a signal transducer mediation communication between ATP binding site and action or microtubules binding site.For unique loops of myosin, using fluorescent reasonance energy transfer technique, It has been demonstrated that the conformation of the loop M changes during the ATPase cycle, suggesting th that loop M acts as a signal transducer mediating communication between the ATPbinding -and action-binding site.For unique loops of kinesin, the results of molecular biological experiments indicated that the loop L5 in kinesin motor domain determins the gliding velocity of microtubules.

肌球蛋白和驱动蛋白的运动结构域的结构高度保守。因此，这些运动蛋白可能具有共同的通过 ATP 水解产生能量的机制。然而，肌球蛋白和驱动蛋白在每个运动域中都有几个独特的环。这些环的精确功能尚不清楚，但它们可能在确定每种运动蛋白的特性方面发挥作用。在本研究中，利用多种生化和分子生物学技术研究了ATP酶中环的构象变化，实验结果表明环可能作为信号转导器介导ATP结合位点和作用或微管结合位点之间的通讯。 ATP酶循环，表明环M作为介导ATP结合位点和动作结合位点之间通讯的信号转导器。对于驱动蛋白独特的环，分子生物学实验结果表明，驱动蛋白运动域中的环L5决定微管的滑动速度。

项目成果

Maruta, S., Mizukura, Y., Chaen, S.: "Interaction of a New Fluorescent ATP Analogue with Skeletal Muscle Myosin Subfragment-1"J. Biochem.. 131. 905-911 (2002)

Maruta, S.、Mizukura, Y.、Chaen, S.：“新型荧光 ATP 类似物与骨骼肌肌球蛋白亚片段 1 的相互作用”J。

S.Maruta., Y.Mizukura., and S.Chaen.: "Interaction of a New Fluorescent ATP Analogue with Skeleta Muscle Myosin Subfragment-1"J. Biochem.. 131. 905-911 (2002)

S.Maruta.、Y.Mizukura. 和 S.Chaen.：“新型荧光 ATP 类似物与骨骼肌肌球蛋白亚片段 1 的相互作用”J。

H.Shibuya., K.Kondo., N.Kimura., & S.Maruta.: "Formation and Characterization of Kinesin ADP Fluorometal Complexes"J. Biochem.. 132. 573-579 (2002)

H.涩谷.、K.近藤.、N.木村.、

Maruta, S., Saitoh, J., Asakura, T.: "Analysis of conformational change at the unique loop adjacent to the ATP binding site of smooth muscle myosin using fluorescent probe"J. Biochem.. 127. 199-204 (2000)

Maruta, S.、Saitoh, J.、Asakura, T.：“使用荧光探针分析邻近平滑肌肌球蛋白 ATP 结合位点的独特环的构象变化”J.

Maruta et al.: "Solution structure of myosin-ADP-MgFn ternary complex by fluorescent probes and small-angle synchrotron X-ray scattering"J.Biochem.. 128. 677-684 (2000)

Maruta 等人：“通过荧光探针和小角同步加速器 X 射线散射的肌球蛋白-ADP-MgFn 三元复合物的溶液结构”J.Biochem.. 128. 677-684 (2000)