Abstract Myosin V and myosin VI are two classes of two-headed molecular motors of the myosin superfamily that move processively along helical actin filaments in opposite directions. Here we present a hand-over-hand model for their processive movements. In the model, the moving direction of a dimeric molecular motor is automatically determined by the relative orientation between its two heads at free state and its head's binding orientation on track filament. This determines that myosin V moves toward the barbed end and myosin VI moves toward the pointed end of actin. During the moving period in one step, one head remains bound to actin for myosin V whereas two heads are detached for myosin VI: the moving manner is determined by the length of neck domain. This naturally explains the similar dynamic behaviours but opposite moving directions of myosin VI and mutant myosin V (the neck of which is truncated to only one-sixth of the native length). Because of different moving manners, myosin VI and mutant myosin V exhibit significantly broader step-size distribution than native myosin V. However,all the three motors give the same mean step size of $\sim $36nm (the pseudo-repeat of actin helix). All these theoretical results are in agreement with previous experimental ones.
Received: 28 May 2004
Revised: 12 November 2004
Accepted manuscript online:
Near-zero thermal expansion in β-CuZnV2O7 in a large temperature range Yaguang Hao(郝亚光), Hengli Xie(谢恒立), Gaojie Zeng(曾高杰), Huanli Yuan(袁焕丽), Yangming Hu(胡杨明), Juan Guo(郭娟), Qilong Gao(高其龙), Mingju Chao(晁明举), Xiao Ren(任霄), and Er-Jun Liang(梁二军). Chin. Phys. B, 2022, 31(4): 046502.
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