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 approximately 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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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC16890 | PMC |
http://dx.doi.org/10.1073/pnas.97.17.9482 | DOI Listing |
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