How kinesin waits between steps

Teppei Mori, Ronald D. Vale () and Michio Tomishige
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Teppei Mori: The University of Tokyo
Ronald D. Vale: University of California, San Francisco, California 94158, USA
Michio Tomishige: The University of Tokyo

Nature, 2007, vol. 450, issue 7170, 750-754

Abstract: Double header The ubiquitous motor protein kinesin has been extensively studied yet a basic mechanistic question remained unanswered — is kinesin bound by both or just one of its heads to the microtubule as it waits between each 8-nm step? Mori et al. have now developed single-molecule fluorescence resonance energy transfer (smFRET) sensors to track the motor as it moves along microtubules. They find that at physiological concentrations of ATP, kinesin waits in-between steps in a two-headed bound state, whereas at lower ATP concentrations, a one-head bound state predominates.

Date: 2007
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DOI: 10.1038/nature06346

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