• Login
    View Item 
    •   Home
    • UMass Chan Student Research and Publications
    • Morningside Graduate School of Biomedical Sciences
    • Morningside Graduate School of Biomedical Sciences Scholarly Publications
    • View Item
    •   Home
    • UMass Chan Student Research and Publications
    • Morningside Graduate School of Biomedical Sciences
    • Morningside Graduate School of Biomedical Sciences Scholarly Publications
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of eScholarship@UMassChanCommunitiesPublication DateAuthorsUMass Chan AffiliationsTitlesDocument TypesKeywordsThis CollectionPublication DateAuthorsUMass Chan AffiliationsTitlesDocument TypesKeywords

    My Account

    LoginRegister

    Help

    AboutSubmission GuidelinesData Deposit PolicySearchingAccessibilityTerms of UseWebsite Migration FAQ

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    The motor domain determines the large step of myosin-V

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Authors
    Tanaka, Hiroto
    Homma, Kazuaki
    Iwane, Atsuko Hikikoshi
    Katayama, Eisaku
    Ikebe, Reiko
    Saito, Junya
    Yanagida, Toshio
    Ikebe, Mitsuo
    UMass Chan Affiliations
    Department of Physiology
    Graduate School of Biomedical Sciences
    Document Type
    Journal Article
    Publication Date
    2002-01-24
    Keywords
    Actins; Adenosine Triphosphate; Animals; Biomechanics; Chickens; Escherichia coli; Models, Biological; Molecular Motor Proteins; Mutation; Myosin Type V; Protein Structure, Tertiary; Recombinant Fusion Proteins; Xenopus
    Life Sciences
    Medicine and Health Sciences
    
    Metadata
    Show full item record
    Link to Full Text
    http://dx.doi.org/10.1038/415192a
    Abstract
    Class-V myosin proceeds along actin filaments with large ( approximately 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.
    Source
    Nature. 2002 Jan 10;415(6868):192-5. Link to article on publisher's site
    DOI
    10.1038/415192a
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/32666
    PubMed ID
    11805840
    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1038/415192a
    Scopus Count
    Collections
    Morningside Graduate School of Biomedical Sciences Scholarly Publications

    entitlement

     
    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Lamar Soutter Library, UMass Chan Medical School | 55 Lake Avenue North | Worcester, MA 01655 USA
    Quick Guide | escholarship@umassmed.edu
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.