Abstract
Kinesin-1, kinesin-2 and kinesin-5 are three families of a superfamily of motor proteins; which can walk processively on microtubule filaments by hydrolyzing ATP. It was experimentally shown that while the three kinesin dimers show similar feature on the force dependence of velocity, they show rather different features on the force dependence of run length. However, why the three families of kinesins show these rather different features is unclear. Here, we computationally studied the movement dynamics of the three dimers based on our proposed model. The simulated results reproduce well the available experimental data on the force dependence of velocity and run length. Moreover, the simulated results on the velocity and run length for the three dimers with altered neck linker lengths are also in quantitative agreement with the available experimental data. The studies indicate that the three families of kinesins show much similar movement mechanism and the rather different features on the force dependence of run length arise mainly from the difference in rate constants of the ATPase activity and neck linker docking. Additionally, the asymmetric (limping) movement dynamics of the three families of homodimers with and without altered neck linker lengths are studied, providing predicted results.
Highlights
Kinesins are a superfamily of motor proteins capable of walking on microtubule (MT) filaments by using the energy from ATP hydrolysis to perform diverse biological functions, including the transport of intracellular cargoes, responsibility of chromosome segregation during cell division, etc
Do the three dimers possess different movement mechanisms, giving the different features on the force dependence of the run length? If the three dimers share the similar mechanism, what are the factors that induce the different features on the force dependence of the run length? what are the origins that shortening the NLs of the three dimers increases their run lengths? The main purpose of this paper is to clarify these unclear issues, which would have a significant implication to the movement mechanisms of the kinesin dimers
By considering a very small but non-zero distance along the x direction, which is called biased distance and is denoted by δ
Summary
Kinesins are a superfamily of motor proteins capable of walking on microtubule (MT) filaments by using the energy from ATP hydrolysis to perform diverse biological functions, including the transport of intracellular cargoes, responsibility of chromosome segregation during cell division, etc. [1]. Kinesin-1 ( called conventional kinesin) consists of two identical motor domains (heads) that are connected together by a coiled-coil stalk through their neck linkers (NLs) (each containing 14 amino acids (AAs)) [3]. KIF3A/B is one of the most abundant kinesin-2 family motors [5] It is composed of two non-identical heads, KIF3A and KIF3B, which are connected together by the coiled-coil stalk through their NLs (each containing 17 AAs). Eg5, a member of kinesin-5 family, is a homotetrameric kinesin protein [10]. It is composed of two pairs of heads that are arranged anti-parallel and are connected to the opposite ends of a common stalk via their linkers
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