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Related Experiment Videos

Rhinovirus type 14 RNA polymerase complexes.

M M Griffith, C J Gauntt

    Archives of Virology
    |January 1, 1975
    PubMed
    Summary
    This summary is machine-generated.

    Rhinovirus type 14 RNA polymerase complexes are initially membrane-associated but later released into the cytoplasm. This study tracks viral RNA synthesis and polymerase activity over time in infected cells.

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    Area of Science:

    • Virology
    • Molecular Biology
    • Cell Biology

    Background:

    • Rhinovirus type 14 (RV14) infection involves viral RNA replication.
    • Understanding the localization and activity of viral RNA-dependent RNA polymerase is crucial for viral replication studies.

    Purpose of the Study:

    • To investigate the characteristics and localization of RV14 RNA-dependent RNA polymerase complexes during infection.
    • To correlate polymerase activity with viral RNA synthesis rates in infected cells.

    Main Methods:

    • Isolation of microsomal and soluble RNA polymerase complexes from infected KB cells.
    • Measurement of polymerase activities at different time points post-inoculation.
    • Analysis of in vitro RNA products, including size heterogeneity and ribonuclease sensitivity.

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  • Assessment of detergent effects on microsomal RNA polymerase activity.
  • Main Results:

    • Peak polymerase activities were observed at 6-7 hours post-inoculation for microsomal and soluble fractions, respectively.
    • Both activities decreased significantly by 8-9 hours post-inoculation, coinciding with maximal in vivo viral RNA synthesis.
    • Synthesized RNA products were heterogeneous in size and included both ribonuclease-sensitive and resistant forms.
    • Detergent treatment did not alter the RNA synthesis profile of microsomal polymerases.

    Conclusions:

    • RV14 RNA polymerase complexes appear to transition from a membrane-associated state to a soluble cytoplasmic form.
    • This transition may be an irreversible release mechanism.
    • The findings provide insights into the dynamic behavior of viral RNA polymerase during replication.