Identification of a human immunodeficiency virus-1 protease cleavage site within the 66,000 Dalton subunit of reverse transcriptase.
The human immunodeficiency virus-1 reverse transcriptase is a heterodimer of related 51 and 66 kDa subunits. The smaller subunit arises by viral protease-catalyzed cleavage of the carboxy-terminal domain of the 66 kDa species. Comparison of the amino acid composition analyses of the isolated 51 kDa and 66 kDa subunits indicates that the carboxyl terminus of 51 kDa is Phe440. This site was confirmed in vitro using purified recombinant protease and a peptide spanning the postulated cleavage area. The sequence surrounding this site does not show significant homology to other protease cleavage sites in the viral gag and pol precursors; thus, this new information may contribute to our understanding of the sequence specificity of the viral protease.
Graves
M C
MC
Department of Molecular Genetics, Hoffmann-La Roche Inc., Roche Research Center, Nutley, NJ 07110.
Meidel
M C
MC
Pan
Y C
YC
Manneberg
M
M
Lahm
H W
HW
Grüninger-Leitch
F
F
D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000378:metabolism*; D015684:Gene Products, pol / Q000378:metabolism*; D016333:HIV Protease; D015497:HIV-1 / Q000201:enzymology* / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism*; D013379:Substrate Specificity
D015684:Gene Products, pol; D012194:RNA-Directed DNA Polymerase; D010450:Endopeptidases; D016333:HIV Protease