Efficient secretion and processing of heterologous proteins in Saccharomyces cerevisiae is mediated solely by the pre-segment of alpha-factor precursor.
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.
D005822:Genetic Vectors; D011498:Protein Precursors; D011506:Proteins / Q000032:analysis / Q000378:metabolism*; D011993:Recombinant Fusion Proteins; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism
D011498:Protein Precursors; D011506:Proteins; D011993:Recombinant Fusion Proteins