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Isolation and characterization of Rous sarcoma virus recombinant reverse transcriptase dimers.

A P Chernov1, A V Koryagin, V A Ivanov

  • 1Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142292, Russia. cap@ibpm.serpukhov.su

Biochemistry. Biokhimiia
|September 28, 1999
PubMed
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Researchers isolated Rous sarcoma virus (RSV) reverse transcriptase (RT) from E. coli. Different enzyme forms showed varying DNA polymerase and RNase H activities, similar to native RSV RT.

Area of Science:

  • Molecular Biology
  • Virology
  • Enzymology

Background:

  • Reverse transcriptase (RT) is crucial for retroviral replication.
  • Understanding the molecular forms and activities of RT is essential for developing antiviral strategies.
  • Rous sarcoma virus (RSV) provides a model system for studying retroviral enzymes.

Purpose of the Study:

  • To isolate and characterize different molecular forms of RSV reverse transcriptase (RT) expressed in E. coli.
  • To compare the enzymatic activities (DNA polymerase and RNase H) of various RT dimer forms.
  • To assess the similarity of recombinant RSV RT forms to virion-associated RT.

Main Methods:

  • Expression of the Rous sarcoma virus (RSV) pol gene in E. coli using plasmid pMF14.
  • Isolation and purification of different RT molecular forms (alphaalpha, betabeta, alphabeta dimers).

Related Experiment Videos

  • Enzymatic assays to determine DNA polymerase and RNase H activities of purified RT forms.

    • Main Results:

    • Three dimeric forms of RSV RT (alphaalpha, betabeta, alphabeta) were successfully isolated.
    • All three forms exhibited DNA polymerase activity, with relative activities of 1:3:4 for alphaalpha, betabeta, and alphabeta, respectively.
    • RNase H activity was present in betabeta and alphabeta dimers but absent in the alphaalpha dimer.

    Conclusions:

    • The study successfully produced and characterized recombinant RSV RT forms in E. coli.
    • The differential enzymatic activities of the RT dimers provide insights into the functional roles of subunits.
    • The findings suggest that the recombinant betabeta and alphabeta RSV RT dimers closely mimic their native counterparts found in virions.