Published in

National Academy of Sciences, Proceedings of the National Academy of Sciences, 10(101), p. 3444-3449, 2004

DOI: 10.1073/pnas.0307691101

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Kinesin's second step

Journal article published in 2004 by Lisa M. Klumpp, Andreas Hoenger ORCID, Susan P. Gilbert
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

We have identified dimeric kinesin mutants that become stalled on the microtubule after one ATP 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.