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Studies on histone acetyltransferase. Partial purification and basic properties

J E Wiktorowicz, J Bonner

    The Journal of Biological Chemistry
    |November 10, 1982
    PubMed
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    Researchers developed a fast method to purify rat liver histone acetyltransferase (HAT). This enzyme

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Histone acetyltransferase (HAT) plays a crucial role in gene regulation through histone modification.
    • Purification of active HAT enzymes is challenging due to their inherent instability.
    • Understanding HAT properties is essential for deciphering epigenetic mechanisms.

    Purpose of the Study:

    • To develop a rapid and reproducible purification method for rat liver histone acetyltransferase.
    • To characterize the biochemical properties and stability of the purified enzyme.
    • To investigate the substrate specificity and catalytic mechanism of rat liver HAT.

    Main Methods:

    • Nuclei extraction in low salt buffer.
    • Purification using phenyl-Sepharose hydrophobic affinity chromatography, G-200 gel filtration, CM-cellulose ion exchange, and acetyllysine affinity chromatography.

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  • Enzyme characterization including molecular weight determination, stability assays, pH optimum, and kinetic analysis.

    • Main Results:

    • A 96,000 molecular weight rat liver HAT was successfully purified.
    • Enzyme instability was partly attributed to hydrophobic interactions; it is sensitive to heat and sulfhydryl agents.
    • The enzyme requires low Mg2+ or Ca2+ concentrations and exhibits optimal activity at pH 7.5, catalyzing histone acetylation in a specific order (H3 > H4 > H2b > H2a > H1).

    Conclusions:

    • The developed method provides a stable and active form of rat liver HAT.
    • The purified enzyme shares properties with previously reported nuclear HAT isozymes (A and DB).
    • This study offers insights into HAT stability, catalytic mechanism, and potential roles in gene regulation.