tailieunhanh - Báo cáo khoa học: Enhanced peptide secretion by gene disruption of CYM1, a novel protease in Saccharomyces cerevisiae

accharomyces cerevisiaeis a widely used host in the pro-ductionof therapeutic peptides report the identification of a novel endoprotease in S. cerevisiae. It is encoded by the CYM1gene and is specific for the C-terminus of basic residues of heterologously expressed peptides. Gene disruption ofCYM1not only reduced the intracellular proteolysis, but also enhanced the secretion of heterologously expressed peptides such as growth hormone, pro-B-type natriuretic peptide and pro-cholecystokinin | Eur. J. Biochem. 271 4788-4797 2004 FEBS 2004 doi Enhanced peptide secretion by gene disruption of CYM1 a novel protease in Saccharomyces cerevisiae Lars Janson Jens F. Rehfeld and Anders H. Johnsen Department of Clinical Biochemistry Rigshospitalet Copenhagen Denmark Saccharomyces cerevisiae is a widely used host in the production of therapeutic peptides and proteins. Here we report the identification of a novel endoprotease in S. cerevisiae. It is encoded by the CYM1 gene and is specific for the C-terminus of basic residues of heterologously expressed peptides. Gene disruption of CYM1 not only reduced the intracellular proteolysis but also enhanced the secretion of heterologously expressed peptides such as growth hormone pro-B-type natriuretic peptide and pro-cholecystokinin. Cym1p resembles metalloendoproteases of the pitrilysin family with the HXXEH X E 71-77 catalytic domain as seen in insulysin nardilysin and human metalloprotease 1. It is a nuclear encoded protease that localizes to mitochondria without a hydrophobic N-terminal signal sequence or a C-terminal tail-anchor. The protease does not require post-translational processing prior to activation and it contains cytosolic activity that processes peptides designated for the secretory pathway prior to translocation into the endoplasmic reticulum. Keywords cholecystokinin growth hormone metalloprotease proBNP yeast. Saccharomyces cerevisiae is often used for industrial production of recombinant peptides 1 . Secretion of heterologously expressed proteins is obtained by expression of fusion proteins in which the protein of interest is fused to the S. cerevisiae a-factor prepropeptide to direct secretion through the secretory pathway. To enrich the secretion of full length peptides the host strains used are often made protease deficient by inactivation of the vacuolar protease Pep4p and the glycosyl-phophatidylinositol GPI -anchored aspartyl protease Yps1p 2 . Yps1p has been .

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