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Updated: Jul 10, 2026

Growth-based Determination and Biochemical Confirmation of Genetic Requirements for Protein Degradation in Saccharomyces cerevisiae
Published on: February 16, 2015
Efficient secretion and processing of heterologous proteins in Saccharomyces cerevisiae is mediated solely by the
1Biogen S.A., Geneva, Switzerland.
Abstract:
A novel processing site was identified in fusions of the alpha-factor precursor of Saccharomyces cerevisiae following its 19 amino-terminal residues (pre-segment). Fusions of the pre-segment to heterologous proteins, including aminoglycoside phosphotransferase (APH) and human granulocyte-macrophage colony stimulating factor (hGM-CSF), were as efficiently secreted and processed as corresponding pre-pro fusions. Pre- and pre-pro fusions to hGM-CSF were identically N- and O-glycosylated. While pre-pro fusions to interleukin-1 beta were not cleaved, pre-fusions were correctly processed during secretion. The high secretion efficiency of pre-fusions suggests that the pro-segment of the alpha-factor precursor is not required for efficient secretion and processing of protein fusions.
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