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Science 6 July 1990:
Vol. 249. no. 4964, pp. 42 - 47
DOI: 10.1126/science.2142332
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Articles

Science, Vol 249, Issue 4964, 42-47
Copyright © 1990 by American Association for the Advancement of Science

articles

Evidence that the head of kinesin is sufficient for force generation and motility in vitro

JT Yang, WM Saxton, RJ Stewart, EC Raff, and LS Goldstein

Department of Cellular and Developmental Biology, Harvard University, Cambridge, MA 02138.

Kinesin is a mechanochemical protein that converts the chemical energy in adenosine triphosphate into mechanical force for movement of cellular components along microtubules. The regions of the kinesin molecule responsible for generating movement were determined by studying the heavy chain of Drosophila kinesin, and its truncated forms, expressed in Escherichia coli. The results demonstrate that (i) kinesin heavy chain alone, without the light chains and other eukaryotic factors, is able to induce microtubule movement in vitro, and (ii) a fragment likely to contain only the kinesin head is also capable of inducing microtubule motility. Thus, the amino-terminal 450 amino acids of kinesin contain all the basic elements needed to convert chemical energy into mechanical force.


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