Cooperativity of multiple kinesin-1 motors mechanically coupled through a shared load
Cooperativity of multiple kinesin-1 motors mechanically coupled through a shared load
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DOI：
10.1016/j.physd.2009.01.005
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发表时间：
2009-04-01
影响因子：
4
通讯作者：
Meyhoefer, Edgar
中科院分区：
文献类型：
--
作者：
Hendricks, Adam G.;Epureanu, Bogdan I.;Meyhoefer, Edgar
最近使用单分子技术的实验已经表征了在一系列载荷和ATP浓度下体外单个驱动蛋白分子的机械性质。这些实验已经表明，驱动蛋白通过使用布朗运动和ATP水解的能量以双手交替的方式交替推进其每个马达结构域，沿着沿着微管向前移动。我们已经扩展了驱动蛋白的理论分析，通过一个机械模型，能够描述瞬态和稳态行为。需要瞬态动力学来描述外部扰动的影响（例如与其他驱动蛋白分子的相互作用）。定量指标是定制的非线性，非光滑系统，如驱动蛋白的同步特性。这些指标被用来分析模拟结果，并量化的货物连接器刚度，负载，并在两个耦合的马达蛋白的同步油的固有速度的差异的影响。在这里，机械模型和新的分析技术的情况下，两个耦合驱动蛋白马达证明。(C)2009 Elsevier B.V.保留所有权利。
Recent experiments using single-molecule techniques have characterized the mechanical properties of single kinesin molecules in vitro at a range of loads and ATP concentrations. These experiments have shown that kinesin moves processively along microtubules by alternately advancing each of its motor domains in a hand-over-hand fashion, using Brownian motion and the energy from ATP hydrolysis. We have extended the theoretical analysis of kinesin through a mechanistic model that is capable of describing transient and steady-state behavior. Transient dynamics are needed to describe the effect of external perturbations (e.g. interactions with other kinesin molecules). Quantitative metrics are tailored to characterize the synchronization of nonlinear, nonsmooth systems such as kinesin. These metrics are employed to analyze the simulation results and to quantify the effect of the cargo linker stiffness, the load, and the difference in intrinsic velocity oil the synchronization of two coupled motor proteins. Herein, the mechanistic model and the new analysis techniques are demonstrated for the case of two coupled kinesin motors. (C) 2009 Elsevier B.V. All rights reserved.