Abstract
KINESIN, a microtubule-dependent ATPase, is believed to be involved in anterograde axonal transport. The kinesin head, which contains both microtubule and ATP binding sites, has the necessary components for the generation of force and motility1. We have used saturation binding and electron microscopy to examine the interaction of the kinesin motor domain with the microtubule surface and found that binding saturated at one kinesin head per tubulin heterodimer. Both negative staining and cryo-electron microscopy revealed a regular pattern of kinesin bound to the microtubule surface, with an axial repeat of 8 nm. Optical diffraction analysis of decorated microtubules showed a strong layer-line at this spacing, confirming that one kinesin head binds per tubulin heterodimer. The addition of Mg–ATP to the microtubule–kinesin complex resulted in the complete dissociation of kinesin from the microtubule surface.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Yang, J. T., Saxton, W. M., Stewart, R. J., Raff, E. C. & Goldstein, L. S. B. Science 249, 42–47 (1990).
Vale, R. D., Reese, T. S. & Sheetz, M. P. Cell 42, 39–50 (1985).
Scholey, J. M., Porter, M. E., Grissom, P. M. & Mclntosh, J. R. Nature 318, 483–486 (1985).
Brady, S. T. Nature 317, 73–75 (1985).
Kuznetsov, S. A. & Gelfand, V. I. Proc. natn. Acad. Sci. U.S.A. 83, 8530–8534 (1986).
Grimstone, A. V. & Klug, A. J. Cell Sci. 1, 351–362 (1966).
Amos, L. A. & Klug, A. J. Cell Sci. 14, 523–549 (1974).
Kuznetsov, S. A., Vaisberg, Υ. Α., Rothwell, S. W., Murphy, D. B. & Gelfand, V. I. J. biol. Chem. 264, 589–595 (1989).
Ingold, A. L., Cohn, S. A & Scholey, J. M. J. Cell Biol. 107, 2657–2667 (1988).
Laemmli, U. K. Nature 227, 680–685 (1970).
Booy, F. P., Newcomb, W. W., Trus, B. L., Brown, J. C., Baker, T. S. & Steven, A. C. Cell 64, 1007–1015 (1991).
Steven, A. C. & Navia, M. A. Proc. natn. Acad. Sci. U.S.A. 77, 4721–4725 (1980).
Gilbert, S. P. & Johnson, K. A. Biochemistry (in the press).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Harrison, B., Marchese-Ragona, S., Gilbert, S. et al. Decoration of the microtubule surface by one kinesin head per tubulin heterodimer. Nature 362, 73–75 (1993). https://doi.org/10.1038/362073a0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/362073a0
This article is cited by
-
The inchworm episode: Reconstituting the phenomenon of kinesin motility
European Journal for Philosophy of Science (2021)
-
Coupling of kinesin ATP turnover to translocation and microtubule regulation: one engine, many machines
Journal of Muscle Research and Cell Motility (2012)
-
Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin
Nature Structural & Molecular Biology (2008)
-
Pathway of processive ATP hydrolysis by kinesin
Nature (1995)
-
Three-dimensional structure of the kinesin headá¤-microtubule complex
Nature (1995)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
