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Science 26 January 2001:
Vol. 291. no. 5504, pp. 667 - 669
DOI: 10.1126/science.291.5504.667
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Reports

Nucleotide-Dependent Single- to Double-Headed Binding of Kinesin

Kenji Kawaguchi,1 Shin'ichi Ishiwata1234*

The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5'-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5'-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.

1 Department of Physics, School of Science and Engineering;
2 Advanced Research Institute for Science and Engineering;
3 Materials Research Laboratory for Bioscience and Photonics, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan.
4 Core Research for Evolutional Science and Technology (CREST), "Genetic Programming" Team 13, Nogawa 907, Miyamae-ku, Kawasaki 216-0001, Japan.
*   To whom correspondence should be addressed. E-mail: ishiwata{at}mn.waseda.ac.jp

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