Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
Biophys Chem. 2021 Apr;271:106548. doi: 10.1016/j.bpc.2021.106548. Epub 2021 Jan 16.
Kinesin-5 and kinesin-1 proteins are two families of kinesin superfamily molecular motors that can move processively on microtubules powered by ATP hydrolysis. Kinesin-1 is a unidirectional motor. By contrast, some yeast kinesin-5 motors are bidirectional and the directionality can be switched by changing the experimental conditions. Here, on the basis of a common chemomechanical coupling model, the dynamics of kinesin-1 and in particular the dynamics of kinesin-5 is studied theoretically, explaining the available experimental data. For example, the experimental data about different movement directions under different experimental conditions for kinesin-5 are explained well. The origin of why kinesin-1 can only make unidirectional movement and kinesin-5 can make bidirectional movements is revealed. The origin of mutations or deletions of several structural elements affecting the directionality of kinesin-5 is revealed. Moreover, some predicted results for kinesin-5 are provided.
驱动蛋白-5 和驱动蛋白-1 蛋白是驱动蛋白超家族分子马达的两个家族，它们可以在微管上进行 ATP 水解驱动的定向运动。驱动蛋白-1 是一种单向马达。相比之下，一些酵母驱动蛋白-5 马达是双向的，并且可以通过改变实验条件来切换方向。在这里，基于常见的化学机械偶联模型，从理论上研究了驱动蛋白-1，特别是驱动蛋白-5 的动力学，解释了现有的实验数据。例如，很好地解释了驱动蛋白-5 在不同实验条件下不同运动方向的实验数据。揭示了为什么驱动蛋白-1 只能进行单向运动，而驱动蛋白-5 可以进行双向运动的原因。揭示了几个影响驱动蛋白-5 方向性的结构元素的突变或缺失的原因。此外，还提供了一些对驱动蛋白-5 的预测结果。
