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[Protein-bound mono (adenosine-diphosphate-ribose) levels during the cell cycle of the slime mold Physarum

K Wielckens, W Sachsenmaier, H Hilz

    Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
    |January 1, 1979
    PubMed

    Insights

    Two distinct ADP-ribose (ADPR)-protein conjugate fractions in Physarum polycephalum exhibit differential hydroxylamine sensitivity, indicating separate synthesis during the cell cycle and multiple roles for nuclear ADP-ribosylation.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Context:

    • Investigating post-translational modifications in eukaryotic organisms.
    • Focusing on ADP-ribosylation, a key regulatory mechanism.
    • Utilizing the slime mold Physarum polycephalum as a model system.

    Purpose:

    • To differentiate and characterize ADP-ribose (ADPR)-protein conjugates.
    • To determine the synthesis patterns of these conjugates during the cell cycle.
    • To elucidate the functional diversity of nuclear ADP-ribosylation.

    Summary:

    • Two fractions of ADPR-protein conjugates were identified based on hydroxylamine susceptibility.
    • Independent synthesis pathways were observed: NH2OH-resistant fraction during S phase, NH2OH-sensitive fraction at the S/G2 boundary.
    • These distinct temporal syntheses suggest multiple functions for nuclear ADP-ribosylation.

    Impact:

    • Provides insights into the regulation of ADP-ribosylation.
    • Highlights the complexity of nuclear signaling pathways.
    • Contributes to understanding cell cycle control mechanisms.

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