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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >A common chemomechanical coupling model for orphan and conventional kinesin molecular motors
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A common chemomechanical coupling model for orphan and conventional kinesin molecular motors

机译：孤儿和常规运动型分子电机的公共化学机械耦合模型

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摘要

Orphan and conventional kinesin dimers represent two families of the kinesin superfamily molecular motors. Conventional kinesin, having a 14-residue neck linker (NL) in each head, can step processively on microtubule (MT), with an ATP hydrolysis being coupled with a mechanical stepping under no load. Orphan kinesin phragmoplast-associated kinesin-related protein 2 (PAKRP2) dimer, despite having a NL of 32 residues in each head, can also step processively on MT and exhibits tight chemomechanical coupling under no load. However, the dynamic properties of the wild type PAKRP2 and the mutant one with each NL truncated to 14 residues are very different from those of the wild type conventional kinesin and the mutant one with each NL being replaced by the 32-residue NL from PAKRP2. Here, based on a common chemomechanical coupling model we study computationally the dynamics of the two families of the kinesin dimers, with the simulated results explaining quantitatively the available experimental data. The large differences in the dynamics between the two families of kinesin dimers arise mainly from different rate constants of NL docking and ATPase activity and different weak affinities of the head in ADP state for MT. The studies indicate that both the orphan kinesin PAKRP2 and conventional kinesin use the same mechanism for processive motility.
机译：孤儿和常规的kinesin二聚体代表了kinesin超家族分子电机的两个家庭。在每个头部中具有14-残基的颈部接头（N1）的常规Kinesin可以在微管（MT）上处理，ATP水解与在没有负载下的机械踩踏时。 Orphan Kinesin Phragmoplast相关的Kinesin相关蛋白2（PAKRP2）二聚体，尽管在每个头部具有32个残留物，但也可以在MT上处理，并且在没有负载下表现出紧密的化学机械偶联。然而，野生型PAKRP2和突变体的动态性质与每个NL截短至14个残基的突变物质与野生型常规Kinesin和突变体的动态性质与来自PAKRP2的32-残基NL所取代的每个NL的突变体。这里，基于普通的化学机械耦合模型，我们在计算上研究了Kinesin二聚体的两个系列的动态，模拟结果解释了可用的实验数据。两种Kinesin二聚体系之间的动力学的差异主要来自NL对接和ATPase活性的不同速率常数和MT的ADP状态下的头部不同的弱亲和力。这些研究表明，孤儿Kinesin PAKRP2和常规运动员都使用相同的加工运动机制。

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