Pohlig G, et al. (1991) Influence of yeast proteases on hirudin expression in Saccharomyces cerevisiae. Biomed Biochim Acta 50(4-6):711-6
Abstract: Recombinant desulfatohirudin variant 1 is efficiently expressed and secreted from Saccharomyces cerevisiae. Chemical analysis of the secreted hirudin compounds revealed the presence of the full-length hirudin molecule as well as two degradation products that lack the C-terminal and in addition the penultimate amino acid, respectively. To eliminate the yeast proteases possibly involved in C-terminal hirudin proteolysis, we disrupted either the structural gene for endoprotease yscA (PRA1) or the gene encoding carboxypeptidase yscY (PRC1). Both isogenic mutant strains secreted significantly higher amounts of full-length hirudin as compared to the parental strain. This suggests an involvement of carboxypeptidase yscY in hirudin proteolysis, since both protease disruptions lead to a lack in yscY activity; a yscA mutant accumulates the inactive yscY precursor. However, the strain devoid of protease yscA yielded significantly lower titers of total hirudin than the strain lacking yscY, but containing yscA.
|Status: Published||Type: Journal Article||PubMed ID: 1801748|
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Number of different genes curated to this paper: 2
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