Abstract
Both amyloid-prone cystatin and unstable mutant C94A lysozyme were secreted in wild-type and Δeps1 Saccharomyces cerevisiae cells. Amyloid-prone cystatin secreted at much higher level in Δeps1 cells than that in wild-type yeast. In parallel, the secretion amount of disulfide bond disrupted mutant C94A lysozyme greatly increased in Δeps1 cells although that was apparently low in wild-type yeast cells compared with the secretion amount of wild-type lysozyme. It is interesting that neither the unstable mutant C94A lysozyme nor amyloid-prone cystatin secreted in Δeps1 cells maintained their specific activities. These observations lead to the supposition that yeast cells deficient for the protein disulfide isomerase-family-member EPS1 locus secrete more of labile disulfide-containing model proteins.
Original language | English |
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Pages (from-to) | 2277-2283 |
Number of pages | 7 |
Journal | FEBS Letters |
Volume | 579 |
Issue number | 11 |
DOIs | |
Publication status | Published - Apr 25 2005 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology