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A nuclear protein-modifying enzyme is responsive to ordered chromatin structure.

T R Butt, J F Brothers, C P Giri

    Nucleic Acids Research
    |August 1, 1978
    PubMed
    Summary

    Poly (ADP-ribose) polymerase activity correlates with chromatin structure. Enzyme activity peaks with 8-10 nucleosomes, decreasing as chromatin complexity increases, suggesting a link between ADP-ribosylation and chromatin organization.

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    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Epigenetics

    Background:

    • Poly (ADP-ribose) polymerase (PARP) is a nuclear enzyme involved in DNA repair and chromatin regulation.
    • PARP binds to chromatin, modifying histones including H1 and core nucleosomal histones.

    Purpose of the Study:

    • To investigate the relationship between Poly (ADP-ribose) polymerase activity and chromatin organization.
    • To determine how nucleosome repeat number and chromatin compactness affect PARP specific activity.

    Main Methods:

    • Enzyme activity assays on chromatin fractions with varying nucleosome repeat numbers.
    • Analysis of chromatin particles through resedimentation and dialysis to assess specific activity differences.

    Main Results:

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    • PARP specific activity per unit of DNA is maximal on chromatin with 8-10 nucleosomes.
    • Activity declines and stabilizes with increasing chromatin complexity (higher nucleosome repeat number and compactness).
    • Observed differences in specific activity are intrinsic to the chromatin particles and not due to polymer chain length or degradation.

    Conclusions:

    • ADP-ribosylation is closely linked to chromatin organization.
    • Chromatin structure influences PARP activity, and PARP activity may, in turn, affect chromatin organization.