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Interaction of HIV reverse transcriptase with structures mimicking recombination intermediates.

Aarti Raja1, Jeffrey J DeStefano

  • 1Department of Cell Biology and Molecular Genetics, University of Maryland College Park, College Park 20742, USA.

The Journal of Biological Chemistry
|January 21, 2003
PubMed
Summary

Human immunodeficiency virus (HIV) reverse transcriptase (RT) interacts with recombination intermediates. RT preferentially cleaves donor RNA in a trimeric structure, aided by HIV nucleocapsid protein (NC), protecting acceptor RNA during strand exchange.

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Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Recombination is crucial for viral genome replication.
  • Human immunodeficiency virus (HIV) reverse transcriptase (RT) plays a key role in viral replication and recombination.
  • Strand transfer is a proposed mechanism for HIV recombination involving transient trimeric structures.

Purpose of the Study:

  • To investigate the interactions between HIV RT and model structures of recombination intermediates.
  • To elucidate the role of RT in the strand exchange process during recombination.
  • To determine the effect of HIV nucleocapsid protein (NC) on RT activity during recombination.

Main Methods:

  • Construction of model trimeric structures mimicking recombination intermediates, including replication intermediates and dimeric constituents.

Related Experiment Videos

  • Biochemical assays to assess the interaction of HIV RT with these structures.
  • Analysis of RNA cleavage activity of RT on different RNA regions within the structures.
  • Investigation of the influence of HIV NC on RT-mediated RNA cleavage.

    • Main Results:

    • HIV RT demonstrated the ability to cleave the RNA component of all examined structures.
    • RT exhibited reduced stability when associated with junction substrates.
    • On the trimeric structure, RT preferentially cleaved the donor RNA over the acceptor RNA.
    • HIV NC protein accentuated RT's preference for cleaving the donor RNA region.

    Conclusions:

    • HIV RT primarily associates with the donor RNA portion of the trimeric recombination intermediate.
    • The acceptor RNA is partially protected from cleavage, facilitating strand exchange.
    • This protection mechanism may aid in salvaging replication if DNA dissociates from the cleaved donor RNA.