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Related Experiment Videos

Double-stranded RNA-dependent RNase activity associated with human immunodeficiency virus type 1 reverse

H Ben-Artzi1, E Zeelon, M Gorecki

  • 1BioTechnology General Ltd., Kiryat Weizmann, Rehovot, Israel.

Proceedings of the National Academy of Sciences of the United States of America
|February 1, 1992
PubMed
Summary
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Human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) exhibits a novel RNase D activity, distinct from its known RNase H function. This enzyme specifically cleaves primer binding site RNA, potentially aiding viral replication.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Retroviral replication involves converting viral RNA to DNA using reverse transcriptase (RT).
  • HIV-1 RT possesses DNA polymerase and RNase H activities essential for this process.
  • The primer for HIV-1 reverse transcription is tRNALys.

Purpose of the Study:

  • To investigate an unexpected enzymatic activity observed in recombinant HIV-1 RT.
  • To characterize a novel RNase activity distinct from the known RNase H function of HIV-1 RT.
  • To determine the role of this new activity in the retroviral replication cycle.

Main Methods:

  • Purification and characterization of recombinant HIV-1 RT.
  • Enzymatic assays to detect and analyze RNA cleavage activity.

Related Experiment Videos

  • Gel filtration and ion-exchange chromatography to assess enzyme properties.
  • Sequence analysis of cleaved RNA substrates.

    • Main Results:

    • Recombinant HIV-1 RT demonstrated a specific RNA cleavage activity, termed RNase D, on HIV-1 RNA hybridized to tRNALys.
    • This RNase D activity was distinct from RNase H, with different substrate specificities and products.
    • RNase D activity comigrated with other RT activities and was present in multiple RT preparations.
    • Sequence analysis revealed specific cleavage sites within the primer binding site (PBS) of HIV-1 RNA.

    Conclusions:

    • HIV-1 RT possesses an intrinsic RNase D activity that specifically cleaves the primer binding site RNA.
    • This RNase D activity is likely involved in critical steps of reverse transcription, such as primer displacement or template switching.
    • The discovery of RNase D activity provides new insights into the complex mechanisms of retroviral replication.