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Model for processive movement of myosin V and myosin VI | | Ping Xie
; Shuo-Xing Dou
; Peng-Ye Wang
; | | Date: |
30 Dec 2003 | | Journal: | Chinese Physics, Vol.14, No.4 (2005) 744-752 | | Subject: | Biomolecules | q-bio.BM | | 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 behaviors 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 three motors give the same mean step size of 36 nm (the pseudo-repeat of actin helix). Using the model we study the dynamics of myosin V quantitatively, with theoretical results in agreement with previous experimental ones. | | Source: | arXiv, q-bio.BM/0312044 | | Services: | Forum | Review | PDF | Favorites | |
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