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Evidence that the Head of Kinesin is Sufficient for Force Generation and Motility in Vitro

Joy T. Yang, William M. Saxton, Russell J. Stewart, Elizabeth C. Raff and Lawrence S. B. Goldstein
Science
New Series, Vol. 249, No. 4964 (Jul. 6, 1990), pp. 42-47
Stable URL: http://www.jstor.org/stable/2874581
Page Count: 6
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Evidence that the Head of Kinesin is Sufficient for Force Generation and Motility in Vitro
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Abstract

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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