Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 97, Issue 17, Pages 9482-9486Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.97.17.9482
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Funding
- NIDCD NIH HHS [DC03299, R29 DC003299, R01 DC003299] Funding Source: Medline
- NIGMS NIH HHS [R01 GM033289, GM33289] Funding Source: Medline
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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 approximate to 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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