Abstract
Myosin-V is a molecular motor that moves processively along its actin track. We have used a feedback-enhanced optical trap to examine the stepping kinetics of this movement. By analyzing the distribution of time periods separating discrete ≈36-nm mechanical steps, we characterize the number and duration of rate-limiting biochemical transitions preceding each such step. These data show that myosin-V is a tightly coupled motor whose cycle time is limited by ADP release. On the basis of these results, we propose a model for myosin-V processivity.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 26, 2002, 10:31 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 5:19 p.m.) |
Indexed | 1 month, 2 weeks ago (July 8, 2025, 7:29 a.m.) |
Issued | 25 years ago (Aug. 15, 2000) |
Published | 25 years ago (Aug. 15, 2000) |
Published Online | 25 years ago (Aug. 15, 2000) |
Published Print | 25 years ago (Aug. 15, 2000) |
@article{Rief_2000, title={Myosin-V stepping kinetics: A molecular model for processivity}, volume={97}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.97.17.9482}, DOI={10.1073/pnas.97.17.9482}, number={17}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Rief, Matthias and Rock, Ronald S. and Mehta, Amit D. and Mooseker, Mark S. and Cheney, Richard E. and Spudich, James A.}, year={2000}, month=aug, pages={9482–9486} }