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Related Experiment Videos

Nucleosomes from normal and regenerating rat liver.

M G Ord, L A Stocken

    The Biochemical Journal
    |January 15, 1979
    PubMed
    Summary
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    Micrococcal nuclease digestion of rat liver nuclei releases mononucleosomes. Histone H1, ADP-ribosylated and phosphorylated, is associated with specific nucleosome fractions, indicating its role in chromatin structure and DNA accessibility.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Chromatin Structure

    Background:

    • Histone H1 plays a crucial role in higher-order chromatin structure.
    • Post-translational modifications of histones, such as ADP-ribosylation and phosphorylation, can influence chromatin organization and function.
    • Nucleosome structure and DNA accessibility are key determinants of gene regulation.

    Purpose of the Study:

    • To investigate the association of modified histone H1 with specific nucleosome fractions released by micrococcal nuclease digestion.
    • To examine the phosphorylation and ADP-ribosylation status of histones within different nucleosome particles.
    • To assess the impact of histone H1 on DNA accessibility and thermal stability of chromatin.

    Main Methods:

    • Micrococcal nuclease digestion of isolated rat liver nuclei.

    Related Experiment Videos

  • Separation of nucleosome fractions using gel filtration (Sephadex G-200) and buffer extraction.
  • Analysis of histone modifications (ADP-ribosylation, phosphorylation) using radiolabeling ([gamma-(32)P]ATP, [(3)H]-thymidine, [(3)H]lysine).
  • DNA length determination and thermal denaturation studies.

    • Main Results:

    • Micrococcal nuclease selectively released mononucleosomes associated with ADP-ribosylated histone H1.
    • Two distinct mononucleosome populations were identified: those with dissociated H1 (140 bp DNA) and those with H1 (200 bp DNA).
    • Phosphorylated histone H1 was observed, and phosphorylation of core histones (H2A, H3) was less evident in H1-containing nucleosomes.
    • Newly synthesized histones and DNA were rapidly incorporated into released nucleosomes during S-phase.
    • Removal of histone H1 and non-histone proteins increased DNA's susceptibility to thermal denaturation.

    Conclusions:

    • ADP-ribosylated and phosphorylated histone H1 is selectively associated with specific nucleosome fractions.
    • Histone H1 content influences DNA accessibility and chromatin stability.
    • These findings highlight the dynamic nature of histone modifications and their role in regulating chromatin structure during DNA replication.