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