The Antiparallel Coiled-Coil Domain Allows Multiple Forward Step Sizes of Myosin X,The Journal of Physical Chemistry Letters

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The Antiparallel Coiled-Coil Domain Allows Multiple Forward Step Sizes of Myosin X
The Journal of Physical Chemistry Letters ( IF 4.8 ) Pub Date : 2023-05-18 , DOI: 10.1021/acs.jpclett.3c00512
Quang Quan Nguyen ₁ , Yangbo Zhou ₂ , Man Sze Cheng ₁ , Xianan Qin ₁ , Harry Chun Man Cheng ₂ , Xiaoyan Liu ₃ , H Lee Sweeney ₃ , Hyokeun Park _{1,

2,

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Affiliation

Myosin X forms an antiparallel dimer and moves processively on actin bundles. How the antiparallel dimer affects the stepping mechanism of myosin X remains elusive. Here, we generated several chimeras using domains of myosin V and X and performed single-molecule motility assays. We found that the chimera containing the motor domain from myosin V and the lever arm and antiparallel coiled-coil domain from myosin X has multiple forward step sizes and moves processively, similar to full-length myosin X. The chimera containing the motor domain and lever arm from myosin X and the parallel coiled-coil from myosin V takes steps of ∼40 nm at lower ATP concentrations but was nonprocessive at higher ATP concentrations. Furthermore, mutant myosin X with four mutations in the antiparallel coiled-coil domain failed to dimerize and was nonprocessive. These results imply that the antiparallel coiled-coil domain is necessary for multiple forward step sizes of myosin X.

中文翻译：

反平行螺旋结构域允许肌球蛋白 X 的多个前向步长

肌球蛋白 X 形成反平行二聚体并在肌动蛋白束上进行性移动。反平行二聚体如何影响肌球蛋白 X 的步进机制仍然难以捉摸。在这里，我们使用肌球蛋白 V 和 X 的结构域生成了几个嵌合体，并进行了单分子运动测定。我们发现包含来自肌球蛋白 V 的运动域和来自肌球蛋白 X 的杠杆臂和反平行卷曲螺旋域的嵌合体具有多个向前步长和连续移动，类似于全长肌球蛋白 X。包含运动域和杠杆的嵌合体来自肌球蛋白 X 的臂和来自肌球蛋白 V 的平行卷曲螺旋在较低的 ATP 浓度下采取约 40 nm 的步骤，但在较高的 ATP 浓度下是非进行性的。此外，在反平行卷曲螺旋结构域中具有四个突变的突变体肌球蛋白 X 无法二聚化并且是非进行性的。

更新日期：2023-05-18

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