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Related Experiment Videos

Adenosine diphosphate ribosylated histones.

M G Ord, L A Stocken

    The Biochemical Journal
    |March 1, 1977
    PubMed
    Summary
    This summary is machine-generated.

    Rat liver nuclei incorporate radioactivity into histones, particularly histone 2B, and non-histone proteins when incubated with [adenine-3H]NAD. This suggests ADP-ribosylation modifies histone properties and localization within the nucleus.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • Histones are crucial for DNA packaging in eukaryotic cells.
    • Post-translational modifications of histones regulate gene expression and chromatin structure.
    • Nicotinamide adenine dinucleotide (NAD) is a substrate for various enzymatic reactions, including ADP-ribosylation.

    Purpose of the Study:

    • To investigate the incorporation of radioactivity from [adenine-3H]NAD into rat liver nuclear proteins.
    • To identify which histone and non-histone proteins are modified.
    • To characterize the nature of the modification and its effect on histone properties.

    Main Methods:

    • Incubation of isolated rat liver nuclei with [adenine-3H]NAD.
    • In vivo administration of [14C]adenine to rats and subsequent isolation of liver and thymus nuclei.

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  • Enzymatic digestion (Pronase, leucine aminopeptidase) of labeled histones.
  • Acid hydrolysis of nucleotide products.
  • Analysis of radioactivity incorporation and distribution.

    • Main Results:

    • Histones 2A and 2B, along with histone 1, incorporated 3H radioactivity from [adenine-3H]NAD.
    • Non-histone proteins and some histones 1 and 3 released into the supernatant also showed radioactivity.
    • In vivo [14C]adenine labeling revealed radioactivity in histones 1 and 3.
    • Digestion of histone 3 yielded ADP-ribose and serine phosphate, indicating ADP-ribosylation.
    • Serine phosphate was also detected in modified histones 2A and 2B.
    • ADP-ribosylated histones 1 and 3 exhibited increased release from nuclei and higher in vivo uptakes of [32P]Pi and [3H]lysine.

    Conclusions:

    • Rat liver nuclei can incorporate ADP-ribose moieties onto histones, particularly histone 2B.
    • ADP-ribosylation affects histone properties, leading to easier release from the nucleus.
    • The modification involves serine phosphate linkages in histones 2A, 2B, and 3.
    • ADP-ribosylation may influence histone turnover and accessibility within the chromatin structure.