Abstract
Saccharomyces cerevisiae is a widely used host for the expression of eukaryotic proteins. However, due to problems such as poor recognition of foreign signal sequences, improper processing and poor secretion, alternative eukaryotic expression systems such as Pichia pastoris have been recently developed.1 The fission yeast Schizosaccharomyces pombe resembles higher eukaryotes in several aspects such as transcriptional regulation, splicing and glycosylation and may therefore serve as a good model system for expression of proteins from higher eukaryotes.2 Several mammalian promoters including SV4o3 and CMV4 are expressed well in this yeast and some mammalian introns are spliced.3In addition, S. pombe has secreted glycoproteins with with terminal galactose6, 7 residues, not found in other yeasts. Furthermore, unlike S. cerevisiae, indigenous secretory proteins in S. pombe such as acid phosphatase are known to be secreted into the culture medium8-10 which simplifies production and analysis of the secreted protein.
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Sambamurti, K. (1997). Expression and Secretion of Mammalian Proteins in Schizosaccharomyces pombe . In: Giga-Hama, Y., Kumagai, H. (eds) Foreign Gene Expression in Fission Yeast: Schizosaccharomyces pombe . Biotechnology Intelligence Unit. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-03472-9_10
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DOI: https://doi.org/10.1007/978-3-662-03472-9_10
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