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Related Experiment Videos

Polymorphic assembly of subtilisin-cleaved tubulin.

E A White, P R Burton, R H Himes

    Cell Motility and the Cytoskeleton
    |January 1, 1987
    PubMed
    Summary

    Limited proteolysis of tubulin using subtilisin releases C-terminal peptides, enabling assembly into various structures like microtubules and rings. This cleavage mimics the effects of microtubule-associated proteins, suggesting charge neutralization is key for tubulin assembly.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Structural Biology

    Background:

    • Tubulin is the primary component of microtubules, essential for cell structure and division.
    • Tubulin assembly is regulated by various factors, including post-translational modifications and small molecules.
    • The C-terminal regions of tubulin subunits are highly acidic and play a role in assembly regulation.

    Purpose of the Study:

    • To investigate the effects of limited proteolysis on tubulin assembly.
    • To understand the role of C-terminal peptides in tubulin polymerization.
    • To compare the assembly-promoting effects of proteolysis with other known agents.

    Main Methods:

    • Limited proteolysis of tubulin using subtilisin at 37°C.
    • Analysis of tubulin assembly under different conditions (GTP, GDP, vinblastine, Zn2+).

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  • Comparison of assembly properties between undigested and proteolyzed tubulin.

    • Main Results:

    • Subtilisin cleavage releases C-terminal peptides from alpha- and beta-tubulin.
    • Proteolyzed tubulin assembles into polymorphic structures (microtubules, rings, spirals) without additional factors.
    • Assembly of undigested tubulin into rings and spirals requires microtubule-associated proteins, high Mg2+, or polycations.
    • Both proteolysis and addition of charged substances promote assembly by neutralizing C-terminal charges.
    • Both forms of tubulin form protofilament sheets in the presence of Zn2+, indicating C-terminal regions are not essential for Zn2+-induced sheet formation.

    Conclusions:

    • Limited proteolysis of tubulin with subtilisin alters its assembly properties.
    • The acidic C-terminal peptides of tubulin are critical regulators of its assembly.
    • Cleavage of these peptides mimics the action of assembly-promoting agents by neutralizing charge.
    • The C-terminal regions are not involved in the binding of Zn2+ for sheet formation.