Abstract
This chapter describes the use of two different yeast promoters to direct the synthesis of interferon (IFN)-α and IFN-γ. The yeast Saccharomyces cerevisae has been used for hundreds of years as an industrial microorganism, having proven its utility in both brewing and baking. Yeast has been utilized in the laboratory for many decades as a model system for the study of many cellular processes. Since the development of molecular cloning techniques in microorganisms, yeast has become increasingly popular for the study of heterologous gene expression. As a eukaryote, yeast cells potentially possess much of the cellular machinery necessary for the expression of foreign eukaryotic genes and for the proper modification of the gene product. Yeast vectors for foreign gene expression contain certain requisite features. The elements of the vector are generally derived from yeast and bacteria to permit the propagation of the plasmid in both. Because APase is a secreted enzyme in yeast, the pYE71 vectors with IFN-αA and IFN-γ might be expected to direct secretion of interferon, but little or no activity is detected in media from induced cells carrying these plasmids. However, there is evidence that the presence of the signal peptide does effect the cellular location of the interferon.
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