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A correction to this article has been published: J. Cell Biol. 153 (7) 1521
Published online 28 May 2001. doi:10.1083/jcb.153.5.1121
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© The Rockefeller University Press, 0021-9525/2001//1121 $5.00
The Journal of Cell Biology, Volume 153, Number 5, , 2001 1121-1126

Report

The Yeast Class V Myosins, Myo2p and Myo4p, Are Nonprocessive Actin-Based Motors



Samara L. Reck-Petersona,b, Matthew J. Tyskaa, Peter J. Novickb, and Mark S. Moosekera,b,c

a Department of Molecular, Cellular, and Developmental Biology,
b Department of Cell Biology, Yale University, New Haven, Connecticut 06520
c Department of Pathology, Yale University, New Haven, Connecticut 06520
Department of Molecular, Cellular, and Developmental Biology, Yale University, KBT 352, P.O. Box 208103, New Haven, CT 06520-8103.(203) 432-6161(203) 431-3468

mark.mooseker{at}yale.edu

The motor properties of the two yeast class V myosins, Myo2p and Myo4p, were examined using in vitro motility assays. Both myosins are active motors with maximum velocities of 4.5 µm/s for Myo2p and 1.1 µm/s for Myo4p. Myo2p motility is Ca2+ insensitive. Both myosins have properties of a nonprocessive motor, unlike chick myosin-Va (M5a), which behaves as a processive motor when assayed under identical conditions. Additional support for the idea that Myo2p is a nonprocessive motor comes from actin cosedimentation assays, which show that Myo2p has a low affinity for F-actin in the presence of ATP and Ca2+, unlike chick brain M5a. These studies suggest that if Myo2p functions in organelle transport, at least five molecules of Myo2p must be present per organelle to promote directed movement.

Key Words: myosin-V • cytoskeleton • in vitro motility • processive motor • cerevisiae

© 2001 The Rockefeller University Press

Abbreviations used in this paper: CaM, calmodulin; M5a, myosin-Va.


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