Multicopy Overexpression of Bovine Pancreatic Trypsin Inhibitor Saturates the Protein Folding and Secretory Capacity of Saccharomyces cerevisiae
Identifieur interne : 001843 ( Istex/Checkpoint ); précédent : 001842; suivant : 001844Multicopy Overexpression of Bovine Pancreatic Trypsin Inhibitor Saturates the Protein Folding and Secretory Capacity of Saccharomyces cerevisiae
Auteurs : R. Parekh [États-Unis] ; K. Forrester [États-Unis] ; D. Wittrup [États-Unis]Source :
- Protein Expression and Purification [ 1046-5928 ] ; 1995.
Abstract
Abstract: Bovine pancreatic trypsin inhibitor (BPTI) was expressed and secreted from a synthetic gene as a model system for the study of protein folding and secretion in Saccharomyces cerevisiae. The efficiency of different leader sequences in directing BPTI secretion was examined, and up to 11 μg/ml of active BPTI was secreted. In some fusion constructs, inefficient proteolytic processing by Kex2p, Ste13p, and signal peptidase were observed immediately adjacent to the BPTI N terminus. Insertion of dipeptide spacers improved endoproteolytic processing substantially but the level of secretion was unchanged, Overexpression from a 2-μm multicopy vector results in essentially unchanged BPTI secretion as compared to expression from a single copy centromere vector. BPTI expressed from a multicopy vector accumulates intracellularly in an unfolded form, indicating that available secretory chaperones and foldases can be saturated by increasing the rate of BPTI synthesis.
Url:
DOI: 10.1006/prep.1995.1071
Affiliations:
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<front><div type="abstract" xml:lang="en">Abstract: Bovine pancreatic trypsin inhibitor (BPTI) was expressed and secreted from a synthetic gene as a model system for the study of protein folding and secretion in Saccharomyces cerevisiae. The efficiency of different leader sequences in directing BPTI secretion was examined, and up to 11 μg/ml of active BPTI was secreted. In some fusion constructs, inefficient proteolytic processing by Kex2p, Ste13p, and signal peptidase were observed immediately adjacent to the BPTI N terminus. Insertion of dipeptide spacers improved endoproteolytic processing substantially but the level of secretion was unchanged, Overexpression from a 2-μm multicopy vector results in essentially unchanged BPTI secretion as compared to expression from a single copy centromere vector. BPTI expressed from a multicopy vector accumulates intracellularly in an unfolded form, indicating that available secretory chaperones and foldases can be saturated by increasing the rate of BPTI synthesis.</div>
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