Site-specific cleavage of a fusion protein by renin.
A double-stranded synthetic oligonucleotide that codes for an amino acid sequence specifically recognized and cleaved by the endopeptidase, renin, was inserted into a plasmid expression vector. The double-stranded oligonucleotide was placed at the junction between the sequences coding for two distinct domains of a fusion protein. The vector used for this analysis expressed a 190-kD Epstein-Barr virus membrane antigen (EBV-MA)-beta-galactosidase (beta-gal) fusion protein (Beisel et al., 1985). The resultant novel protein product expressed by the new construction can be cleaved specifically by renin to yield two distinct polypeptides, EBV-MA and beta-gal, corresponding to the two domains of the original fusion protein product.
Haffey
M L
ML
Department of Microbial Biochemistry, Squibb Institute for Medical Research, Princeton, NJ 08543.
Lehman
D
D
Boger
J
J
D000956:Antigens, Viral; D001483:Base Sequence; D005822:Genetic Vectors; D004854:Herpesvirus 4, Human / Q000276:immunology; D009841:Oligonucleotides / Q000138:chemical synthesis; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism*; D012083:Renin / Q000378:metabolism*; D014763:Viral Matrix Proteins; D001616:beta-Galactosidase
D000956:Antigens, Viral; C037662:EBV-associated membrane antigen, Epstein-Barr virus; D009841:Oligonucleotides; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; D014763:Viral Matrix Proteins; D001616:beta-Galactosidase; D012083:Renin