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首页> 外文期刊>Nature >DIRECT OBSERVATION OF SINGLE KINESIN MOLECULES MOVING ALONG MICROTUBULES
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DIRECT OBSERVATION OF SINGLE KINESIN MOLECULES MOVING ALONG MICROTUBULES

机译：直接观察沿微管运动的单个驱动分子

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摘要

KINESIN is a two-headed motor protein that powers organelle transport along microtubules(1). Many ATP molecules are hydrolysed by kinesin for each diffusional encounter with the microtubule(2,3). Here we report the development of a new assay in which the processive movement of individual fluorescently labelled kinesin molecules along a microtubule can be visualized directly; this observation is achieved by low-background total internal reflection fluorescence microscopy(4) in the absence of attachment of the motor to a cargo (for example, an organelle or bead). The average distance travelled after a binding encounter with a microtubule is 600 nm, which reflects a similar to 1% probability of detachment per mechanical cycle, Surprisingly, processive movement could still be observed at salt concentrations as high as 0.3 M NaCl. Truncated kinesin molecules having only a single motor domain do not show detectable processive movement, which is consistent with a model in which kinesin's two force-generating heads operate by a hand-over-hand mechanism. [References: 24]
机译：激肽是一种双向运动蛋白，可促进细胞器沿着微管的运输（1）。每次与微管的扩散相遇时，驱动蛋白会水解许多ATP分子（2,3）。在这里，我们报告了一种新的检测方法的开发，其中单个荧光标记的驱动蛋白分子沿微管的进行性运动可以直接观察到；这种观察是通过低背景全内反射荧光显微镜（4）来实现的，并且没有将马达连接到货物上（例如，细胞器或珠子）。与微管结合后经过的平均距离为600 nm，这反映出每个机械周期的分离概率接近1％。令人惊讶的是，在高达0.3 M NaCl的盐浓度下仍可观察到进行性运动。仅具有单个运动域的截短的驱动蛋白分子未显示可检测的进行性运动，这与驱动蛋白的两个力产生头通过交接机制操作的模型相一致。 [参考：24]

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