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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A Mobile Kinesin-head Intermediate During The Atp-waiting State
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A Mobile Kinesin-head Intermediate During The Atp-waiting State

机译：Atp等待状态中的移动驱动蛋白头中间体

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摘要

Kinesin is a motor protein that uses the energy from ATP hydrolysis to move intracellular cargoes along microtubules. It contains 2 identical motor domains, or heads, that coordinate their mechano-chemical cycles to move processively along microtubules. The molecular mechanism of coordination between head domains remains unclear, partly because of the lack of structural information on critical intermediates of the kinesini mechano-chemical cycle. A point of controversy has been whether before ATP binding, in the so called ATP-waiting state, 1 or 2 motor domains are bound to the microtubule. To address this issue, here we use ensemble and single molecule fluorescence polarization microscopy (FPM) to determine the mobility and orientation of the kinesini heads at different ATP concentrations and in heterodimeric constructs with microtubule binding impaired in 1 head. We found evidence for a mobile head during the ATP-waiting state. We incorporate our results into a model for kinesin translocation that accounts well for many reported experimental results.
机译：驱动蛋白是一种运动蛋白，它利用ATP水解产生的能量沿微管移动细胞内货物。它包含2个相同的运动域或磁头，它们协调它们的机械化学循环，以沿着微管进行性移动。头部结构域之间协调的分子机制仍然不清楚，部分原因是缺乏关于开尼西尼机械化学循环关键中间体的结构信息。争论的焦点是在ATP结合之前，在所谓的ATP等待状态下，是将1或2个运动域结合到微管上。为了解决这个问题，这里我们使用整体和单分子荧光偏振显微镜（FPM）来确定在不同的ATP浓度下以及在1个头部的微管结合受到损害的异二聚体构建物中，kinesini头部的迁移率和方向。我们找到了在ATP等待状态下移动头部的证据。我们将我们的结果纳入驱动蛋白易位模型，该模型很好地说明了许多报道的实验结果。

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