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Human immunodeficiency virus 1 reverse transcriptase. Template binding, processivity, strand displacement synthesis,

H E Huber1, J M McCoy, J S Seehra

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.

The Journal of Biological Chemistry
|March 15, 1989
PubMed
Summary

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Human immunodeficiency virus 1 (HIV-1) reverse transcriptase kinetics were analyzed. This enzyme exhibits processive DNA synthesis, with rates and processivity influenced by template type and conditions, enabling synthesis beyond template length.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Virology

Background:

  • Reverse transcriptase (RT) is a key enzyme in retroviral replication.
  • Understanding HIV-1 RT kinetics is crucial for developing antiviral therapies.

Purpose of the Study:

  • To investigate the kinetic properties of purified HIV-1 reverse transcriptase.
  • To characterize DNA synthesis processivity and template utilization.

Main Methods:

  • Enzymatic assays using purified HIV-1 reverse transcriptase.
  • Kinetic analysis of DNA synthesis on various template types.
  • Characterization of enzyme-template complex formation and stability.

Main Results:

  • HIV-1 RT forms stable complexes with primer-templates, with initiation dependent on Mg2+ and dTTP.

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  • DNA synthesis is processive, with rates of 10-15 nucleotides/s on poly(rA) templates.
  • Processivity varies significantly with template, and RT can perform strand displacement and utilize multiple templates.

    • Conclusions:

    • HIV-1 RT exhibits complex kinetic behavior influencing DNA synthesis.
    • Template-dependent processivity and strand switching are key features of HIV-1 RT.
    • These findings provide insights into retroviral DNA replication mechanisms.