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Papers In Press, published online ahead of print July 14, 2004
Neurology Dept., University of Alabama at Birmingham, Birmingham, AL 35294
Corresponding Author: stevensr{at}uab.edu
Cytoplasmic transport is mediated by a group of molecular motors that typically work in isolation, under conditions where they must move their cargos long distances without dissociating from their tracks. This processive behavior requires specific adaptations of motor enzymology to meet these unique physiologic demands. One of these involves the ability of the two heads of a processive motor to communicate their structural states to each other. In this study, we examine a processive motor from the myosin superfamily--myosin V. We have measured the kinetics of nucleotide release, phosphate release, and of the weak-to-strong transition as this motor interacts with actin, and have used these studies to develop a model of how myosin V functions as a transport motor. Surprisingly both heads release phosphate rapidly upon the initial encounter with an actin filament, suggesting that there is little or no intramolecular strain associated with this step. However, ADP release can be affected by both forward and rearward strain, and under steady state conditions is essentially prevented in the lead head until the rear head detaches. Many of these features are remarkably like those underlying kinesin’s processive movement on microtubules, supporting our hypothesis that different molecular motors satisfy the requirement for processive movement in similar ways, regardless of their particular family of origin.
J. Biol. Chem, 10.1074/jbc.M402583200
Submitted on March 8, 2004
Revised on June 28, 2004
Accepted on July 13, 2004
A model of myosin V processivity
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