Chicken myosin-V is a two-headed, barbed-end-directed motor capable of moving actin filaments at rates up to 400 nm/s, distinct from myosins-I and myosins-II.
Chicken myosin-V is a member of a recently recognized class of myosins distinct from both the myosins-I and the myosins-II. We report here the purification, electron microscopic visualization, and motor properties of a protein of this class. Myosin-V molecules consist of two heads attached to an approximately 30 nm stalk that ends in a globular region of unknown function. Myosin-V binds to and decorates F-actin, has actin-activated magnesium-ATPase activity, and is a barbed-end-directed motor capable of moving actin filaments at rates of up to 400 nm/s. Myosin-V does not form filaments. Each myosin-V heavy chain is associated with approximately four calmodulin light chains as well as two less abundant proteins of 23 and 17 kd.
Cheney et al. (1993) studied this question. Chicken myosin-V was evaluated on Motor properties and structure of myosin-V. Chicken myosin-V is a two-headed, barbed-end-directed motor capable of moving actin filaments at rates up to 400 nm/s, distinct from myosins-I and myosins-II.
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