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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments
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Multiple tail domain interactions stabilize nonmuscle myosin II bipolar filaments

机译：多个尾域相互作用可稳定非肌球蛋白II双极丝

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摘要

Contractile force transduction by myosin II derives from its assembly into bipolar filaments. The coiled-coil tail domain of the myosin II heavy chain mediates filament assembly, although the mechanism is poorly understood. Tail domains contain an alternating electrostatic repeat, yet only a small region of the tail (termed the "assembly domain") is typically required for assembly. Using computational analysis, mutagenesis, and electron microscopy we discovered that the assembly domain does not function through self-interaction as previously thought. Rather, the assembly domain acts as a unique, positively charged interaction surface that can stably contact multiple complementary, negatively charged surfaces in the upstream tail domain. The relative affinities of the assembly domain to each complementary interaction surface sets the characteristic molecular staggers observed in myosin II filaments. Together these results explain the relationship between the charge repeat and assembly domain in stabilizing myosin bipolar filaments.
机译：肌球蛋白Ⅱ的收缩力转导源自其组装成双极细丝。肌球蛋白II重链的卷曲螺旋尾结构域介导细丝组件，虽然机制尚不清楚。尾部区域包含交替的静电重复，但是通常只需要尾部的一小部分区域（称为“组装区域”）即可。通过计算分析，诱变和电子显微镜，我们发现组装域不像以前所认为的那样通过自我相互作用起作用。而是，组装域充当独特的带正电荷的相互作用表面，可以稳定地接触上游尾域中的多个互补的带负电荷的表面。组装结构域对每个互补相互作用表面的相对亲和力设置了在肌球蛋白II细丝中观察到的特征性分子交错。这些结果共同解释了稳定肌球蛋白双极细丝时电荷重复和组装结构域之间的关系。

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