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.
Zervos
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Division of Molecular and Cell Biology Research, Lilly Research Laboratories, Indianapolis, Indiana 46285.
Hassell
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Van Frank
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Lai
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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