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Structure of the poly(G) polymerase component of the bacteriophage f2 replicase

N V Fedoroff, N D Zinder

    Proceedings of the National Academy of Sciences of the United States of America
    |August 1, 1971
    PubMed

    Insights

    Researchers purified a rifampicin-resistant poly(G) polymerase from f2-infected cells. This enzyme is likely part of the f2 replicase, showing similar resistance and synthesizing viral RNA.

    Area of Science:

    • Molecular Biology
    • Virology
    • Enzymology

    Background:

    • The f2 phage replicase is crucial for viral RNA synthesis.
    • Understanding the components of the viral replicase is essential for comprehending viral replication mechanisms.

    Purpose of the Study:

    • To purify and characterize a rifampicin-resistant poly(G) polymerase from f2-infected cells.
    • To investigate the potential role of this polymerase in f2 viral RNA replication.

    Main Methods:

    • Purification of poly(G) polymerase from f2 sus 11-infected cells.
    • Assay of polymerase activity using denatured f2 RNA template.
    • Electrophoretic analysis of purified protein components.

    Main Results:

    • A rifampicin-resistant poly(G) polymerase was successfully purified.
    • Partially purified polymerase demonstrated replicase activity, synthesizing f2 RNA.
    • Highly purified polymerase contained a protein identical to the viral replicase product.

    Conclusions:

    • The purified poly(G) polymerase is likely a component of the f2 replicase.
    • This finding contributes to understanding the molecular machinery of f2 viral replication.

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