Nucleotide-dependent single- to double-headed binding of kinesin

K. Kawaguchi, S. Ishiwata

    研究成果: Article

    103 引用 (Scopus)

    抄録

    The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5′-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5′-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.

    元の言語English
    ページ(範囲)667-669
    ページ数3
    ジャーナルScience
    291
    発行部数5504
    DOI
    出版物ステータスPublished - 2001 1 26

    Fingerprint

    Kinesin
    Nucleotides
    Hand
    Adenylyl Imidodiphosphate
    Microtubules
    Adenosine Triphosphate
    Head
    Optical Tweezers
    Elastic Modulus
    Adenosine Diphosphate
    Hydrolysis

    ASJC Scopus subject areas

    • General

    これを引用

    Nucleotide-dependent single- to double-headed binding of kinesin. / Kawaguchi, K.; Ishiwata, S.

    :: Science, 巻 291, 番号 5504, 26.01.2001, p. 667-669.

    研究成果: Article

    Kawaguchi, K. ; Ishiwata, S. / Nucleotide-dependent single- to double-headed binding of kinesin. :: Science. 2001 ; 巻 291, 番号 5504. pp. 667-669.
    @article{1de0e88a38874bd5a59255f6087399ea,
    title = "Nucleotide-dependent single- to double-headed binding of kinesin",
    abstract = "The motility of kinesin motors is explained by a {"}hand-over-hand{"} model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5′-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5′-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.",
    author = "K. Kawaguchi and S. Ishiwata",
    year = "2001",
    month = "1",
    day = "26",
    doi = "10.1126/science.291.5504.667",
    language = "English",
    volume = "291",
    pages = "667--669",
    journal = "Science",
    issn = "0036-8075",
    publisher = "American Association for the Advancement of Science",
    number = "5504",

    }

    TY - JOUR

    T1 - Nucleotide-dependent single- to double-headed binding of kinesin

    AU - Kawaguchi, K.

    AU - Ishiwata, S.

    PY - 2001/1/26

    Y1 - 2001/1/26

    N2 - The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5′-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5′-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.

    AB - The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5′-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5′-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model.

    UR - http://www.scopus.com/inward/record.url?scp=0035951471&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=0035951471&partnerID=8YFLogxK

    U2 - 10.1126/science.291.5504.667

    DO - 10.1126/science.291.5504.667

    M3 - Article

    C2 - 11158681

    AN - SCOPUS:0035951471

    VL - 291

    SP - 667

    EP - 669

    JO - Science

    JF - Science

    SN - 0036-8075

    IS - 5504

    ER -