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Related Experiment Videos

Nucleosomal particles open as the histone core becomes hyperacetylated.

J Bode, M M Gómez-Lira, H Schröter

    European Journal of Biochemistry
    |February 15, 1983
    PubMed
    Summary

    Hyperacetylation of histone proteins in lymphoblastoid cells alters nucleosomal particle structure. This modification impacts particle mobility and conformational flexibility, distinct from the effects of high-mobility-group (HMG) proteins.

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    Area of Science:

    • Molecular Biology
    • Epigenetics
    • Chromatin Structure

    Background:

    • Histone acetylation is a key epigenetic modification regulating gene expression.
    • Nucleosomal particles are the basic units of chromatin, influencing DNA accessibility.
    • The role of histone acetylation in nucleosomal particle heterogeneity and conformation requires further elucidation.

    Purpose of the Study:

    • To investigate the impact of histone hyperacetylation on nucleosomal particle structure and electrophoretic behavior.
    • To differentiate the effects of histone acetylation from those of non-histone proteins like HMG 14 and 17.

    Main Methods:

    • Isolation of nucleosomal particles from lymphoblastoid cells treated with the deacetylase inhibitor butyrate.
    • Non-denaturing gel electrophoresis to analyze nucleosomal particle heterogeneity.

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  • Analysis of monomers free from histone H1 and high-mobility-group (HMG) proteins 14 and 17.

    • Main Results:

    • Nucleosomal particles in a hyperacetylated state exhibit heterogeneity not solely due to non-histone proteins.
    • Subfractionation of histone H1 and HMG-depleted monomers occurs based on the degree of core histone acetylation.
    • Hyperacetylation leads to reduced electrophoretic mobility and increased conformational freedom of nucleosomal particles.

    Conclusions:

    • Histone hyperacetylation significantly influences nucleosomal particle conformation and electrophoretic properties.
    • The conformational changes induced by hyperacetylation are distinct from those mediated by HMG proteins.
    • Understanding these structural dynamics is crucial for comprehending epigenetic regulation of chromatin.