REVERSE TRANSCRIPTASE-ASSOCIATED RIBONUCLEASE-H ACTIVITY AS A TARGET FOR ANTIVIRAL CHEMOTHERAPY

The availability of highly purified recombinant enzymes and model hete ropolymeric nucleic acid substrates now allows more precise evaluation of the ribonuclease H (RNase H) activity associated with human immuno deficiency virus (HIV) reverse transcriptase. In addition to degrading the RNA-DNA replicative intermediate, this C-terminal domain of aroun d 130 residues supports highly specialized events that cannot be compl emented by host-coded enzymes during retrovirus replication. RNase H a ctivity should therefore be considered a plausible candidate for thera peutic intervention. Events during HIV replication requiring precise R Nase H-mediated hydrolysis, the methodologies available to study these events, and their potential for therapeutic intervention are reviewed here.