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Related Experiment Videos

Reverse transcriptase-associated ribonuclease H does not require zinc for catalysis

M J Modak, A Srivastava

    The Journal of Biological Chemistry
    |June 10, 1979
    PubMed
    Summary
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    1,10-Phenanthroline, a zinc chelating agent, does not inhibit retroviral reverse transcriptase-associated RNase H activity. Zinc is not involved in template-primer binding or nucleic acid hydrolysis by cellular and viral RNase H enzymes.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • 1,10-Phenanthroline is a known inhibitor of DNA polymerase activity.
    • The role of zinc in the function of RNase H, particularly in retroviruses, is not fully understood.

    Purpose of the Study:

    • To investigate the effect of 1,10-phenanthroline on the reverse transcriptase-associated RNase H activity of retroviruses.
    • To determine the involvement of zinc in template-primer binding and nucleic acid hydrolysis by RNase H enzymes.

    Main Methods:

    • Enzyme inhibition assays using retroviral reverse transcriptase and cellular RNase H.
    • Kinetic studies to analyze substrate binding and enzyme activity.

    Main Results:

    • 1,10-Phenanthroline did not inhibit the RNase H activity associated with retroviral reverse transcriptase.

    Related Experiment Videos

  • Kinetic data suggest zinc is not involved in template-primer binding by reverse transcriptase.
  • Cellular RNase H and viral RNase H-II were also resistant to 1,10-phenanthroline inhibition.

    • Conclusions:

    • Zinc does not appear to play a role in the RNase H activity of retroviral reverse transcriptase.
    • The findings imply that zinc is not essential for nucleic acid hydrolysis by various RNase H enzymes.