Enhancement of HIV-1 proteinase activity by HIV-1 reverse transcriptase.
HIV-1 reverse transcriptase (RT) was found to increase the activity of HIV-1 proteinase in vitro and in eukaryotic cells. The effect of RT on proteinase activity was dose-dependent and independent of pH or salt concentration. The cleavage of sequences corresponding to all the naturally occurring cleavage sites that could be tested in vitro was enhanced. The effect of RT on cleavage was greatest at the cleavage site between RT and integrase. The enhancement of viral proteinase activity by the virus RT may contribute to regulation of the order and/or efficiency of cleavage at different sites during virus replication and maturation.
Goobar-Larsson
L
L
Microbiology and Tumorbiology Center (MTC), Karolinska Institute, Stockholm, Sweden.
Luukkonen
B G
BG
Unge
T
T
Schwartz
S
S
Utter
G
G
Strandberg
B
B
Oberg
B
B
D001483:Base Sequence; D004789:Enzyme Activation; D016333:HIV Protease / Q000378:metabolism*; D054303:HIV Reverse Transcriptase; D015497:HIV-1 / Q000201:enzymology*; D006367:HeLa Cells; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides; D009994:Osmolar Concentration; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism*
D009838:Oligodeoxyribonucleotides; D054303:HIV Reverse Transcriptase; D012194:RNA-Directed DNA Polymerase; D016333:HIV Protease