Abstract
Class V myosins are actin-based molecular motors involved in vesicular and organellar transport. Single myosin V molecules move processively along F-actin, taking several 36-nm steps for each diffusional encounter. Here we have measured the mechanical interactions between mouse brain myosin V and rabbit skeletal F-actin. The working stroke produced by a myosin V head is ∼25 nm, consisting of two separate mechanical phases (20 + 5 nm). We show that there are preferred myosin binding positions (target zones) every 36 nm along the actin filament, and propose that the 36-nm steps of the double-headed motor are a combination of the working stroke (25 nm) of the bound head and a biased, thermally driven diffusive movement (11 nm) of the free head onto the next target zone. The second phase of the working stroke (5 nm) acts as a gate — like an escapement in a clock, coordinating the ATPase cycles of the two myosin V heads. This mechanism increases processivity and enables a single myosin V molecule to travel distances of several hundred nanometres along the actin filament.
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Acknowledgements
We thank E. Harvey for technical assistance, J. A. Hammer III for kindly supplying the MV clone, J. C. Sparrow, D. C. S. White, R. S. Adelstein, J. Trinick, P. J. Knight and E. Homsher for critical reading of the manuscript, and BBSRC, the Royal Society, the Wellcome Trust and the NIH for grant support.
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Veigel, C., Wang, F., Bartoo, M. et al. The gated gait of the processive molecular motor, myosin V. Nat Cell Biol 4, 59–65 (2002). https://doi.org/10.1038/ncb732
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DOI: https://doi.org/10.1038/ncb732
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