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Related Experiment Videos

Zinc binding to tubulin.

J E Hesketh

    The International Journal of Biochemistry
    |January 1, 1983
    PubMed
    Summary

    This study investigated zinc binding to tubulin, revealing two distinct binding sites. High-affinity zinc binding to tubulin was found to be sensitive to N-ethyl maleimide.

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    Area of Science:

    • Biochemistry
    • Cell Biology
    • Molecular Biology

    Background:

    • Tubulin is the main protein of microtubules, essential for cell structure and division.
    • Zinc is a vital trace element involved in numerous cellular processes.
    • Understanding zinc-tubulin interactions is crucial for comprehending zinc's role in cellular functions.

    Purpose of the Study:

    • To quantify zinc binding to tubulin.
    • To characterize the affinity and stoichiometry of zinc-tubulin binding sites.
    • To investigate the effect of N-ethyl maleimide on zinc binding.

    Main Methods:

    • Incubation of purified microtubules with radioactive 65Zn.
    • Quantification of 65Zn retained by tubulin using DEAE Sephadex chromatography.
    • Assessment of N-ethyl maleimide's inhibitory effect on zinc binding.

    Main Results:

    • Two classes of zinc binding sites on tubulin were identified: one with very low affinity and another with higher affinity.
    • The higher affinity site binds approximately 0.86 g-atoms of zinc per mole of tubulin.
    • A dissociation constant (Kd) of approximately 110 microM was determined for the higher affinity site.
    • 2 mM N-ethyl maleimide inhibited zinc binding to the higher affinity site by 50%.

    Conclusions:

    • Tubulin possesses distinct high- and low-affinity sites for zinc binding.
    • The higher affinity zinc-tubulin interaction is characterized by a Kd of ~110 microM.
    • N-ethyl maleimide suggests a potential role for cysteine residues in high-affinity zinc binding to tubulin.

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