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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Contribution of the myosin VI tail domain to processive stepping and intramolecular tension sensing
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Contribution of the myosin VI tail domain to processive stepping and intramolecular tension sensing

机译：肌球蛋白VI尾结构域对进行性步进和分子内张力传感的贡献

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摘要

Myosin VI is proposed to act as both a molecular transporter and as an anchor in vivo. A portion of the molecule C-terminal to the canonical lever arm, termed the medial tail (MT), has been proposed to act as either a lever arm extension or as a dimerization motif. We describe constructs in which the MT is interrupted by a glycine-rich molecular swivel. Disruption of the MT results in decreased processive run lengths measured using single-molecule fluorescence microscopy and a decreased step size under applied load as measured in an optical trap. We used single-molecule gold nanoparticle tracking and optical trapping to examine the mechanism of coordination between the heads of dimeric myosin VI. We detect two rate-limiting kinetic processes at low (<200 micromolar) ATP concentrations. Our data can be explained by a model in which intramolecular tension greatly increases the affinity of the lead head for ADP, likely by slowing ADP release from the lead head. This mechanism likely increases both the motor's processivity and its ability to act as an anchor under physiological conditions.
机译：提出了肌球蛋白VI在体内既充当分子转运蛋白又充当锚。有人提出规范杆臂的C端分子的一部分，称为内侧尾（MT），可充当杆臂延伸或二聚化基序。我们描述了其中MT被富含甘氨酸的分子转环中断的构造。 MT的破坏导致使用单分子荧光显微镜测得的连续运行时间缩短，并在光阱中测得的施加负载下步长减小。我们使用单分子金纳米粒子跟踪和光学陷阱来检查二聚肌球蛋白六的头之间的协调机制。我们在低（<200微摩尔）ATP浓度下检测到两个限速动力学过程。我们的数据可以用一个模型来解释，其中分子内张力极大地增加了铅头对ADP的亲和力，很可能是通过减慢ADP从铅头的释放来实现的。这种机制可能会增加电动机的工作能力及其在生理条件下充当锚的能力。

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