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; Mitsuo Ikebe

doi:10.1038/415192a

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, Mitsuo Ikebe

Otolaryngology

Research output: Contribution to journal › Article › peer-review

117 Scopus citations

Abstract

Class-V myosin proceeds along actin filaments with large (∼36 nm) steps. 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 model, 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). 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.

Original language	English (US)
Pages (from-to)	192-195
Number of pages	4
Journal	Nature
Volume	415
Issue number	6868
DOIs	https://doi.org/10.1038/415192a
State	Published - 2002

Funding

We thank W. Raffelsberger for providing the PCR protocols for RARb2 promoter amplification, and N. Potier and A. van Dorsselaer for the ESI-MS analysis. We are grateful to C. Peluso-Iltis and V. Chavant for help in protein purification, C. Erb for expression vectors and A. Pornon for technical assistance. We thank W. Bourguet for critically reading this manuscript and Y. Lutz and C. Egly for antibodies. BMS-labelled retinoids/rexinoids were provided by C. Zusi, and CD3254 and AGN192870 by U. Reichert and S. Michel. This work was supported by the Institut National de la Santé et de la Recherche Médicale, the Centre National de La Recherche Scientifique, the HoÃpital Universitaire de Strasbourg, the European Community and Bristol-Myers Squibb. We are grateful to N. Jenkins for providing cDNA fragments of mouse myosin-V. We thank colleagues at the Single Molecule Processes Project, University of Massachusetts Medical School, and Osaka University for discussions, and J. West for critically reading the manuscript. This work was supported by grants from the National Institute of Health to M.I.

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10.1038/415192a

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title = "The motor domain determines the large step of myosin-V",

abstract = "Class-V myosin proceeds along actin filaments with large (∼36 nm) steps. 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 model, 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). 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.",

author = "Hiroto Tanaka and Kazuaki Homma and Iwane, {Atsuko Hikikoshi} and Eisaku Katayama and Reiko Ikebe and Junya Saito and Toshio Yanagida and Mitsuo Ikebe",

note = "Funding Information: We thank W. Raffelsberger for providing the PCR protocols for RARb2 promoter amplification, and N. Potier and A. van Dorsselaer for the ESI-MS analysis. We are grateful to C. Peluso-Iltis and V. Chavant for help in protein purification, C. Erb for expression vectors and A. Pornon for technical assistance. We thank W. Bourguet for critically reading this manuscript and Y. Lutz and C. Egly for antibodies. BMS-labelled retinoids/rexinoids were provided by C. Zusi, and CD3254 and AGN192870 by U. Reichert and S. Michel. This work was supported by the Institut National de la Sant{\'e} et de la Recherche M{\'e}dicale, the Centre National de La Recherche Scientifique, the Ho{\~A}pital Universitaire de Strasbourg, the European Community and Bristol-Myers Squibb. Funding Information: We are grateful to N. Jenkins for providing cDNA fragments of mouse myosin-V. We thank colleagues at the Single Molecule Processes Project, University of Massachusetts Medical School, and Osaka University for discussions, and J. West for critically reading the manuscript. This work was supported by grants from the National Institute of Health to M.I.",

year = "2002",

doi = "10.1038/415192a",

language = "English (US)",

volume = "415",

pages = "192--195",

journal = "Nature",

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T1 - The motor domain determines the large step of myosin-V

AU - Tanaka, Hiroto

AU - Homma, Kazuaki

AU - Iwane, Atsuko Hikikoshi

AU - Katayama, Eisaku

AU - Ikebe, Reiko

AU - Saito, Junya

AU - Yanagida, Toshio

AU - Ikebe, Mitsuo

N1 - Funding Information: We thank W. Raffelsberger for providing the PCR protocols for RARb2 promoter amplification, and N. Potier and A. van Dorsselaer for the ESI-MS analysis. We are grateful to C. Peluso-Iltis and V. Chavant for help in protein purification, C. Erb for expression vectors and A. Pornon for technical assistance. We thank W. Bourguet for critically reading this manuscript and Y. Lutz and C. Egly for antibodies. BMS-labelled retinoids/rexinoids were provided by C. Zusi, and CD3254 and AGN192870 by U. Reichert and S. Michel. This work was supported by the Institut National de la Santé et de la Recherche Médicale, the Centre National de La Recherche Scientifique, the HoÃpital Universitaire de Strasbourg, the European Community and Bristol-Myers Squibb. Funding Information: We are grateful to N. Jenkins for providing cDNA fragments of mouse myosin-V. We thank colleagues at the Single Molecule Processes Project, University of Massachusetts Medical School, and Osaka University for discussions, and J. West for critically reading the manuscript. This work was supported by grants from the National Institute of Health to M.I.

PY - 2002

Y1 - 2002

N2 - Class-V myosin proceeds along actin filaments with large (∼36 nm) steps. 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 model, 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). 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.

AB - Class-V myosin proceeds along actin filaments with large (∼36 nm) steps. 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 model, 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). 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.

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JF - Nature

IS - 6868

ER -

The motor domain determines the large step of myosin-V

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