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单个肌球蛋白头部沿着肌动蛋白丝以5.3纳米的规则步长移动。

A single myosin head moves along an actin filament with regular steps of 5.3 nanometres.

作者信息

Kitamura K, Tokunaga M, Iwane A H, Yanagida T

机构信息

Yanagida BioMotron Project, ERATO, JST, Mino, Osaka, Japan.

出版信息

Nature. 1999 Jan 14;397(6715):129-34. doi: 10.1038/16403.

Abstract

Actomyosin, a complex of actin filaments and myosin motor proteins, is responsible for force generation during muscle contraction. To resolve the individual mechanical events of force generation by actomyosin, we have developed a new instrument with which we can capture and directly manipulate individual myosin subfragment-1 molecules using a scanning probe. Single subfragment-1 molecules can be visualized by using a fluorescent label. The data that we obtain using this technique are consistent with myosin moving along an actin filament with single mechanical steps of approximately 5.3 nanometres; groups of two to five rapid steps in succession often produce displacements of 11 to 30 nanometres. This multiple stepping is produced by a single myosin head during just one biochemical cycle of ATP hydrolysis.

摘要

肌动球蛋白是由肌动蛋白丝和肌球蛋白运动蛋白组成的复合物,负责肌肉收缩过程中的力产生。为了解决肌动球蛋白产生力的各个机械事件,我们开发了一种新仪器,利用该仪器我们可以使用扫描探针捕获并直接操纵单个肌球蛋白亚片段-1分子。单个亚片段-1分子可以通过荧光标记进行可视化。我们使用该技术获得的数据与肌球蛋白沿着肌动蛋白丝以约5.3纳米的单个机械步长移动一致;连续两到五步的快速步长通常会产生11到30纳米的位移。这种多步移动是由单个肌球蛋白头部在ATP水解的一个生化循环中产生的。

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