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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
New Series, Vol. 249, No. 4964 (Jul. 6, 1990), pp. 42-47
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/2874581
Page Count: 6
You can always find the topics here!Topics: Microtubules, Amino acids, Plasmids, Molecules, Drosophila, Cell extracts, Mechanical forces, Molecular chains, Complementary DNA, Quaternary ammonium compounds
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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.
Science © 1990 American Association for the Advancement of Science