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Covalent association of protein with replicative form DNA of parvovirus H-1

D Revie, B Y Tseng, R H Grafstrom

    Proceedings of the National Academy of Sciences of the United States of America
    |November 1, 1979
    PubMed

    Insights

    Autonomous parvovirus H-1 replicative form DNA forms a protein complex in infected cells. This protein is associated with DNA ends, but not found in the virus itself.

    Area of Science:

    • Molecular Biology
    • Virology
    • Biochemistry

    Background:

    • Autonomous parvoviruses, like H-1, possess a double-stranded replicative form (RF) DNA.
    • Understanding viral DNA replication and protein interactions is crucial in virology.

    Purpose of the Study:

    • To investigate the nature of protein-DNA complexes associated with H-1 parvovirus RF DNA.
    • To characterize the protein's association with viral DNA during replication.

    Main Methods:

    • Isolation of RF DNA from infected cells.
    • Analysis of protein association with viral DNA fragments.
    • Buoyant density measurements to estimate protein size.

    Main Results:

    • RF DNA of H-1 parvovirus was isolated as a covalent protein complex.
    • The protein was found on most or all RF DNA molecules, including replicating ones.
    • Protein association was specific to 5'-terminal endonuclease Hae III fragments of both viral and complementary strands.
    • Estimated protein size is 60,000-70,000 daltons based on buoyant density shifts.
    • No protein-DNA complex was detected in H-1 virions.

    Conclusions:

    • A specific protein covalently binds to the ends of H-1 parvovirus RF DNA during replication.
    • This protein is integral to the viral DNA replication machinery within infected cells.
    • The absence of this complex in virions suggests a role limited to the intracellular replication cycle.

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