| Literature DB >> 10944217 |
M Rief1, R S Rock, A D Mehta, M S Mooseker, R E Cheney, J A Spudich.
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 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.Entities:
Mesh:
Substances:
Year: 2000 PMID: 10944217 PMCID: PMC16890 DOI: 10.1073/pnas.97.17.9482
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205