Abstract
We have used poly(A)-agarose as an immobilized template to identify certain binding interactions which occur during polymerization of DNA and to analyze the mode of action of several drugs which inhibit oncornavirus DNA synthesis. In addition to demonstrating the binding of Moloney murine leukemia virus DNA polymerase (reverse transcriptase) to this template (both primed and unprimed), we analyzed the effects of nucleotides and several ansamycins (streptoval C, rifamycin SV, rifazone 82, and demethyldimethylbenzylrifampicin) on the stability of these binding interactions. The new poly(A)-agarose system allows more precise identification of the steps in reverse transcription which are targets for drugs previously known to inhibit the over-all reaction; thus this novel approach to the study of DNA polymerization on a solid matrix may afford an alternative rationale for designing antiviral drugs.
ACKNOWLEDGMENTS We thank Dr. J. A. Huberman for his sustained interest in this work, and M. J. Eddy for technical assistance. We also thank Dr. M. Calvin and his colleagues, as well as Dr. R. C. Gallo, for their gifts of ansamycins.
- Copyright © 1977 by Academic Press, Inc.
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