期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 101, 期 10, 页码 3444-3449出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0307691101
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资金
- NIAMS NIH HHS [K02-AR47841, K02 AR047841] Funding Source: Medline
- NIGMS NIH HHS [R37 GM054141, R01 GM054141, GM54141] Funding Source: Medline
We have identified dimeric kinesin mutants that become stalled on the microtubule after one ATIP turnover, unable to bind and hydrolyze ATP at their second site. We have used these mutants to determine the regulatory signal that allows ATP to bind to the forward head, such that processive movement can continue. The results show that phosphate release occurs from the rearward head before detachment, and detachment triggers active-site accessibility for ATP binding at the forward head. This mechanism, in which the rearward head controls the behavior of the forward head, may be conserved among processive motors.
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