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Cleavage of the HIV-1 p66 reverse transcriptase/RNase H by the p9 protease in vitro generates active p15 RNase H.


Arch Virol. 1991;118(3-4):179-88. Unique Identifier : AIDSLINE

The reverse transcriptase/RNase H of HIV-1 is composed of a p66/p51 heterodimer when analyzed from virus particles. A recombinant reverse transcriptase (RT)/RNase H which after purification consisted mainly of p66 was analyzed as substrate of the purified recombinant HIV-1 protease p9 in vitro. The p66 protein if treated with the protease is processed to a stable p66/p51 heterodimer. A p15 protein is a prominent cleavage product which was identified as the carboxyterminal portion of p66 by means of a monoclonal antibody. It exhibits RNase H activity when tested by activated gel analysis. Presence of SDS during the incubation allowed complete degradation of p66 depending on the conditions, which indicates that conformation of a substrate is relevant for cleavage by the HIV-1 protease. A synthetic heptapeptide AET-FYVD derived from the region between RT and RNase H is cleaved efficiently in vitro by the HIV-1 protease at the F'Y junction, and may mimick a natural cleavage site. P66/p51 heterodimers exhibit higher RT and RNase H activities than p66 when renatured from polyacrylamide gels.

Chromatography, High Pressure Liquid Endoribonucleases/*METABOLISM Gene Products, pol/*METABOLISM HIV Protease/METABOLISM HIV-1/*ENZYMOLOGY Oligopeptides/CHEMICAL SYNTHESIS/METABOLISM RNA-Directed DNA Polymerase/*METABOLISM Sodium Dodecyl Sulfate/PHARMACOLOGY Support, Non-U.S. Gov't JOURNAL ARTICLE


Information in this article was accurate in October 30, 1991. The state of the art may have changed since the publication date. This material is designed to support, not replace, the relationship that exists between you and your doctor. Always discuss treatment options with a doctor who specializes in treating HIV.