The motor domain determines the large step of myosin-V

Hiroto Tanaka, Kazuaki Homma, Atsuko Hikikoshi Iwane, Eisaku Katayama, Reiko Ikebe, Junya Saito, Toshio Yanagida () and Mitsuo Ikebe ()
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Hiroto Tanaka: Single Molecule Processes Project, ICORP, JST
Kazuaki Homma: University of Massachusetts Medical School
Atsuko Hikikoshi Iwane: Graduate School of Medicine Osaka University
Eisaku Katayama: Institute of Medical Science, The University of Tokyo
Reiko Ikebe: University of Massachusetts Medical School
Junya Saito: University of Massachusetts Medical School
Toshio Yanagida: Single Molecule Processes Project, ICORP, JST
Mitsuo Ikebe: University of Massachusetts Medical School

Nature, 2002, vol. 415, issue 6868, 192-195

Abstract: Abstract Class-V myosin proceeds along actin filaments with large (∼36 nm) steps1,2,3. Myosin-V has two heads, each of which consists of a motor domain and a long (23 nm) neck domain. In accordance with the widely accepted lever-arm model4, it was suggested that myosin-V steps to successive (36 nm) target zones along the actin helical repeat by tilting its long neck (lever-arm)5. To test this hypothesis, we measured the mechanical properties of single molecules of myosin-V truncation mutants with neck domains only one-sixth of the native length. Our results show that the processivity and step distance along actin are both similar to those of full-length myosin-V. Thus, the long neck domain is not essential for either the large steps or processivity of myosin-V. These results challenge the lever-arm model. We propose that the motor domain and/or the actomyosin interface enable myosin-V to produce large processive steps during translocation along actin.

Date: 2002
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DOI: 10.1038/415192a

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