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Related Experiment Videos

Substructural analysis of the microtubule and its polymorphic forms.

K Fujiwara, L G Tilney

    Annals of the New York Academy of Sciences
    |June 30, 1975
    PubMed
    Summary

    Microtubules feature 13 protofilaments. Bridges connect specific protofilaments, and tubulin heterodimers lie parallel to protofilament axes, exposing the colchicine binding site.

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    The Journal of biological chemistry·1992

    Area of Science:

    • Cell biology
    • Structural biology
    • Biochemistry

    Background:

    • Microtubules are essential cytoskeletal components formed by 13 protofilaments.
    • The precise arrangement and connections of microtubule subunits and associated proteins are crucial for their function.

    Purpose of the Study:

    • To elucidate the specific protofilament connections of microtubule bridges.
    • To investigate the subunit arrangement in polymorphic microtubule forms and determine tubulin heterodimer orientation.

    Main Methods:

    • Analysis of thin sections of microtubules fixed with tannic acid.
    • Markham rotations of isolated flagellar axonemes.
    • Geometric analysis of microtubule structures.
    • Examination of low-temperature and vinblastine-induced microtubule polymorphs.

    Main Results:

    • Bridges (spoke, nexin, dynein) connect to specific protofilaments in flagellar axonemes, Centrohelida, and Raphidiophrys.
    • Polymorphic microtubules, including low-temperature and vinblastine-induced forms, exhibit non-linear protofilament arrangements.
    • Vinblastine crystals show hexagonally packed tubules with walls composed of two spiraling protofilaments (180 A separation).

    Conclusions:

    • Microtubule bridges have specific protofilament attachment sites.
    • The tubulin heterodimer is oriented parallel to the protofilament axis, with the colchicine binding site exposed.

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