NDLI: Kinesin-microtubule binding depends on both nucleotide state and loading direction.

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Kinesin-microtubule binding depends on both nucleotide state and loading direction.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kawaguchi, Kenji Toyoshima, Yoko Yano Uemura, Sotaro Ishiwata, Shin'ichi Yajima, Junichiro Edamatsu, Masaki
Description	Author Affiliation: Uemura S ( Department of Physics, School of Science and Engineering, and Advanced Research Institute for Science and Engineering, Waseda University, 3-4-1 Okubo, Shinjuku-ku, Tokyo 169-8555, Japan.);
Abstract	Kinesin is a motor protein that transports organelles along a microtubule toward its plus end by using the energy of ATP hydrolysis. To clarify the nucleotide-dependent binding mode, we measured the unbinding force for one-headed kinesin heterodimers in addition to conventional two-headed kinesin homodimers under several nucleotide states. We found that both a weak and a strong binding state exist in each head of kinesin corresponding to a small and a large unbinding force, respectively; that is, weak for the ADP state and strong for the nucleotide-free and adenosine 5'-[beta,gamma-imido]triphosphate states. Model analysis showed that (i) the two binding modes in each head could be explained by a difference in the binding energy and (ii) the directional instability of binding, i.e., dependence of unbinding force on loading direction, could be explained by a difference in the characteristic distance for the kinesin-microtubule interaction during plus- and minus-end-directed loading. Both these factors must play an important role in the molecular mechanism of kinesin motility.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Diphosphate Metabolism Kinesin Chemistry Microtubules Animals Brain Dimerization Models, Biological Protein Binding Stress, Mechanical Swine Temperature Time Factors Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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