Characterization of an internally initiated integrase protein of HIV-1 produced in E. coli.
In E. coli cells transformed by an expression vector for the production of the protease (PR) integrase (IN) of HIV-1, three vitally encoded proteins were produced: an 11-kDa protein and a 32-kDa protein identified by immunoassays as the mature PR and IN protein, respectively, and an additional protein 15-kDa in size that reacted strongly with an antiserum recognizing a region in the carboxyl half of the IN protein. The kinetics of its synthesis indicated that it was not a degradation product of p32-IN, rather it probably arose from internal initiation at an AUG codon in the middle of the IN gene. Amino terminal sequence analysis of the first 70 residues demonstrated a perfect match with those predicted from the nucleotide sequence, beginning with the methionine codon at position 154 of the integrase gene.
Division of Molecular and Cell Biology Research, Lilly Research Laboratories, Indianapolis, Indiana 46285.
P
P
Zervos
T
T
Hassell
R
R
Van Frank
M T
MT
Lai
D000595:Amino Acid Sequence; D001483:Base Sequence; D004254:DNA Nucleotidyltransferases / Q000032:analysis / Q000096:biosynthesis* / Q000235:genetics; D004274:DNA, Recombinant / Q000032:analysis; D010450:Endopeptidases / Q000096:biosynthesis / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D015497:HIV-1 / Q000201:enzymology* / Q000235:genetics; D019426:Integrases; D008969:Molecular Sequence Data; D010957:Plasmids; D014170:Transformation, Genetic
D004274:DNA, Recombinant; D004254:DNA Nucleotidyltransferases; D019426:Integrases; D010450:Endopeptidases