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© The Rockefeller University Press, 0021-9525/1998//419 $5.00
The Journal of Cell Biology, Volume 141, Number 2, , 1998 419-430

Articles

Image Reconstructions of Microtubules Decorated with Monomeric and Dimeric Kinesins: Comparison with X-Ray Structure and Implications for Motility



A. Hoenger*, S. Sack{ddagger}, M. Thormählen{ddagger}, A. Marx{ddagger}, J. Müller{ddagger}, H. Gross*, and E. Mandelkow{ddagger}

* Institute of Cell Biology, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland; and {ddagger} Max-Planck-Unit for Structural Molecular Biology, D-22603 Hamburg, Germany

We have decorated microtubules with monomeric and dimeric kinesin constructs, studied their structure by cryoelectron microscopy and three-dimensional image reconstruction, and compared the results with the x-ray crystal structure of monomeric and dimeric kinesin. A monomeric kinesin construct (rK354, containing only a short neck helix insufficient for coiled-coil formation) decorates microtubules with a stoichiometry of one kinesin head per tubulin subunit ({alpha}–β-heterodimer). The orientation of the kinesin head (an anterograde motor) on the microtubule surface is similar to that of ncd (a retrograde motor). A longer kinesin construct (rK379) forms a dimer because of the longer neck helix forming a coiled-coil. Unexpectedly, this construct also decorates the microtubule with a stoichiometry of one head per tubulin subunit, and the orientation is similar to that of the monomeric construct. This means that the interaction with microtubules causes the two heads of a kinesin dimer to separate sufficiently so that they can bind to two different tubulin subunits. This result is in contrast to recent models and can be explained by assuming that the tubulin–kinesin interaction is antagonistic to the coiled-coil interaction within a kinesin dimer.

S. Sack is a recipient of a fellowship from the Friedrich-Ebert Foundation. The project was supported by the Deutsche Forschungsgemeinschaft and the Swiss Science Foundation.

Address all correspondence to Dr. E. Mandelkow, Max-Planck-Unit for Structural molecular Biology, Notkestrasse 85, D-22603 Hamburg, Germany. Tel.: 49-40-8998-2810. Fax: 49-40-8971-6822. E-mail: mandelkow{at}mpasmb.desy.de

A. Hoenger's present address is European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69012 Heidelberg, Germany.

1. Abbreviation used in this paper: AMP-PNP, 5'-adenylylimidodiphosphate.


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