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首页> 外文期刊>Cell biochemistry and biophysics >The Contribution of the C-Terminal Tails of Microtubules in Altering the Force Production Specifications of Multiple Kinesin-1
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The Contribution of the C-Terminal Tails of Microtubules in Altering the Force Production Specifications of Multiple Kinesin-1

机译：微管C末端尾巴在改变多种Kinesin-1的生产能力中的作用

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摘要

The extent to which beta tubulin isotypes contribute to the function of microtubules and the microtubule-driven transport of molecular motors is poorly understood. The major differences in these isotypes are associated with the structure of their C-terminal tails. Recent studies have revealed a few aspects of the C-terminal tails' regulatory role on the activities of some of the motor proteins on a single-molecule level. However, little attention is given to the degree to which the function of a team of motor proteins can be altered by the microtubule's tail. In a set of parallel experiments, we investigated this open question by studying the force production of several kinesin-1 (kinesin) molecular motors along two groups of microtubules: regular ones and those microtubules whose C-terminals are cleaved by subtilisin digestion. The results indicate that the difference between the average of the force production of motors along two types of microtubules is statistically significant. The underlying mechanism of such production is substantially different as well. As compared to untreated microtubules, the magnitude of the binding time of several kinesin-1 is almost three times greater along subtilisin-treated microtubules. Also, the velocity of the group of kinesin molecules shows a higher sensitivity to external loads and reduces significantly under higher loads along subtilisin-treated microtubules. Together, this work shows the capacity of the tails in fine-tuning the force production characteristics of several kinesin molecules.
机译：β微管蛋白同种型有助于微管的功能和分子马达的微管驱动运输的程度尚不清楚。这些同种型的主要差异与其C末端尾巴的结构有关。最近的研究已经揭示了C末端尾部在单分子水平上对某些运动蛋白活性的调节作用的几个方面。然而，很少有人关注微管尾部可以改变一组运动蛋白的功能的程度。在一组平行实验中，我们通过研究沿两组微管的几种kinesin-1（驱动蛋白）分子马达的力产生研究了这个悬而未决的问题：常规微管和那些C末端被枯草杆菌蛋白酶消化切割的微管。结果表明，沿两种类型的微管的电动机平均产力之间的差异具有统计学意义。这种生产的基本机制也大不相同。与未处理的微管相比，沿枯草杆菌蛋白酶处理的微管，几种驱动蛋白-1的结合时间大小几乎是其三倍。同样，驱动蛋白分子组的速度显示出对外部负荷的更高敏感性，并且在较高负荷下沿着枯草杆菌蛋白酶处理的微管明显降低。在一起，这项工作表明尾巴在微调几种驱动蛋白分子的力产生特性方面的能力。

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