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Nucleic Acids Research, 1984, Vol. 12, No. 23 8927-8938
© 1984

MOLECULAR BIOLOGY

Synthesis, secretion and processing of {alpha}-factor-interferon fusion proteins Id yeast

Arjun Singh, June M. Lugovoy, William J. Kohr+ and L.Jeanne Perry+

+Protein Chemistry, Genentech, Inc. 460 Point San Bruno Boulevard, South San Francisco, CA 94080, USA Departments of Molecular Biology Genentech, Inc. 460 Point San Bruno Boulevard, South San Francisco, CA 94080, USA

Received August 31, 1984. Revised October 26, 1984. Accepted October 26, 1984.

A gene fusion consisting of 960 base pairs of 5'-flanking region of the yeast MF{alpha}l gene, 257 base pairs coding for {alpha}-factor prepro sequence, and a modified human IFN-{alpha}l gene was constructed. MAT{alpha} cells containing the chimeric gene synthesized and secreted active IFN-{alpha}l into the growth medium. The secreted interferon molecules contained the last 4 amino acids of {alpha}-factor prepro sequence and the amino acids encoded by the DNA modifications introduced at the beginning of IFN-{alpha}l gene. DNA sequences coding for these amino acids were removed by oligonucleotide-directed in vitro mutagenesis. Yeast cells transformed with expression plasmids containing the altered junction synthesized and secreted human IFN-{alpha}l with the natural NH 2-terminus.


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