dorsal/arxiv
View SchemaModel for processive movement of myosin V and myosin VI
| Authors | Ping Xie, Shuo-Xing Dou, Peng-Ye Wang |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0312044 |
| URL | https://arxiv.org/abs/q-bio/0312044 |
| DOI | 10.1088/1009-1963/14/4/018 |
| Journal | Chinese Physics, Vol.14, No.4 (2005) 744-752 |
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.
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"abstract": "Myosin V and myosin VI are two classes of two-headed molecular motors of the\nmyosin superfamily that move processively along helical actin filaments in\nopposite directions. Here we present a hand-over-hand model for their\nprocessive movements. In the model, the moving direction of a dimeric molecular\nmotor is automatically determined by the relative orientation between its two\nheads at free state and its head\u0027s binding orientation on track filament. This\ndetermines that myosin V moves toward the barbed end and myosin VI moves toward\nthe pointed end of actin. During the moving period in one step, one head\nremains bound to actin for myosin V whereas two heads are detached for myosin\nVI: The moving manner is determined by the length of neck domain. This\nnaturally explains the similar dynamic behaviors but opposite moving directions\nof myosin VI and mutant myosin V (the neck of which is truncated to only\none-sixth of the native length). Because of different moving manners, myosin VI\nand mutant myosin V exhibit significantly broader step-size distribution than\nnative myosin V. However, all three motors give the same mean step size of 36\nnm (the pseudo-repeat of actin helix). Using the model we study the dynamics of\nmyosin V quantitatively, with theoretical results in agreement with previous\nexperimental ones.",
"arxiv_id": "q-bio/0312044",
"authors": [
"Ping Xie",
"Shuo-Xing Dou",
"Peng-Ye Wang"
],
"categories": [
"q-bio.BM"
],
"doi": "10.1088/1009-1963/14/4/018",
"journal_ref": "Chinese Physics, Vol.14, No.4 (2005) 744-752",
"title": "Model for processive movement of myosin V and myosin VI",
"url": "https://arxiv.org/abs/q-bio/0312044"
},
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