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A Generalized Kinetic Model for Coupling between Stepping and ATP Hydrolysis of Kinesin Molecular Motors

机译:驱动蛋白分子马达步进与ATP水解耦合的广义动力学模型

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A general kinetic model is presented for the chemomechanical coupling of dimeric kinesin molecular motors with and without extension of their neck linkers (NLs). A peculiar feature of the model is that the rate constants of ATPase activity of a kinesin head are independent of the strain on its NL, implying that the heads of the wild-type kinesin dimer and the mutant with extension of its NLs have the same force-independent rate constants of the ATPase activity. Based on the model, an analytical theory is presented on the force dependence of the dynamics of kinesin dimers with and without extension of their NLs at saturating ATP. With only a few adjustable parameters, diverse available single molecule data on the dynamics of various kinesin dimers, such as wild-type kinesin-1, kinesin-1 with mutated residues in the NLs, kinesin-1 with extension of the NLs and wild-type kinesin-2, under varying force and ATP concentration, can be reproduced very well. Additionally, we compare the power production among different kinesin dimers, showing that the mutation in the NLs reduces the power production and the extension of the NLs further reduces the power production.
机译:提出了一种通用的动力学模型,用于二聚体驱动蛋白分子马达的化学机械偶联,具有和不具有其颈部连接物(NL)延伸。该模型的一个独特特征是,驱动蛋白头部的ATPase活性速率常数与NL上的菌株无关,这意味着野生型驱动蛋白二聚体的头部和具有NL扩展的突变体具有相同的作用力ATP酶活性的独立速率常数。基于该模型,提出了一种关于驱动蛋白二聚体在饱和ATP下具有和不具有其NL扩展的动力学的力依赖性的分析理论。仅需几个可调整的参数,即可获得有关各种驱动蛋白二聚体动力学的各种可用单分子数据,例如野生型驱动蛋白1,驱动蛋白1(带NL中残基的突变),驱动蛋白1(具有扩展的NLs和野生型)。在变化的力和ATP浓度下,kinesin-2型可以很好地繁殖。此外,我们比较了不同驱动蛋白二聚体之间的发电量,表明NL中的突变降低了发电量,而NL的延伸进一步降低了发电量。

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