肌球蛋白II与F-肌动蛋白的双头结合显示了应变对头部结构的影响。

IF 3 3区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Alimohammad Hojjatian , Dianne W. Taylor , Nadia Daneshparvar , Patricia M. Fagnant , Kathleen M. Trybus , Kenneth A. Taylor
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引用次数: 0

摘要

肌肉中的力量产生是通过肌球蛋白和肌动蛋白的相互作用实现的。活性肌肉中的强结合状态与活性部位结合的Mg·ADP有关;Mg·ADP的释放使ATP重新结合并与肌动蛋白分离。因此,Mg·ADP结合被定位为作为力传感器进行适应。杠杆臂上的机械负荷会影响肌球蛋白释放Mg·ADP的能力,但具体如何做到这一点尚不清楚。在这里,我们使用在Mg·ADP存在下用双头平滑肌肌球蛋白片段修饰的F-肌动蛋白,使用冷冻电镜观察内部供应的张力对成对杠杆臂的影响。成对的头部与两个相邻的肌动蛋白亚基的相互作用预计会使一个杠杆臂处于正应变下,另一个处于负应变下。转换结构域被认为是肌球蛋白头部内最灵活的结构域。相反,我们的研究结果指出,重要轻链和监管轻链之间的重链段是最大结构变化的位置。此外,我们的研究结果表明,当两个头部结合F-肌动蛋白时,作为应变缓解位点的肌球蛋白盘绕螺旋尾部没有大的变化。该方法适用于肌球蛋白家族的双头成员。我们预计,使用双头片段对肌动蛋白-肌球蛋白相互作用的研究能够使用单头片段装饰的通常有噪声的结构域可视化。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Double-headed binding of myosin II to F-actin shows the effect of strain on head structure

Double-headed binding of myosin II to F-actin shows the effect of strain on head structure

Force production in muscle is achieved through the interaction of myosin and actin. Strong binding states in active muscle are associated with Mg·ADP bound to the active site; release of Mg·ADP allows rebinding of ATP and dissociation from actin. Thus, Mg·ADP binding is positioned for adaptation as a force sensor. Mechanical loads on the lever arm can affect the ability of myosin to release Mg·ADP but exactly how this is done is poorly defined. Here we use F-actin decorated with double-headed smooth muscle myosin fragments in the presence of Mg·ADP to visualize the effect of internally supplied tension on the paired lever arms using cryoEM. The interaction of the paired heads with two adjacent actin subunits is predicted to place one lever arm under positive and the other under negative strain. The converter domain is believed to be the most flexible domain within myosin head. Our results, instead, point to the segment of heavy chain between the essential and regulatory light chains as the location of the largest structural change. Moreover, our results suggest no large changes in the myosin coiled coil tail as the locus of strain relief when both heads bind F-actin. The method would be adaptable to double-headed members of the myosin family. We anticipate that the study of actin-myosin interaction using double-headed fragments enables visualization of domains that are typically noisy in decoration with single-headed fragments.

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来源期刊
Journal of structural biology
Journal of structural biology 生物-生化与分子生物学
CiteScore
6.30
自引率
3.30%
发文量
88
审稿时长
65 days
期刊介绍: Journal of Structural Biology (JSB) has an open access mirror journal, the Journal of Structural Biology: X (JSBX), sharing the same aims and scope, editorial team, submission system and rigorous peer review. Since both journals share the same editorial system, you may submit your manuscript via either journal homepage. You will be prompted during submission (and revision) to choose in which to publish your article. The editors and reviewers are not aware of the choice you made until the article has been published online. JSB and JSBX publish papers dealing with the structural analysis of living material at every level of organization by all methods that lead to an understanding of biological function in terms of molecular and supermolecular structure. Techniques covered include: • Light microscopy including confocal microscopy • All types of electron microscopy • X-ray diffraction • Nuclear magnetic resonance • Scanning force microscopy, scanning probe microscopy, and tunneling microscopy • Digital image processing • Computational insights into structure
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