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 |
|---|---|
| Pages (from-to) | 2277-2283 |
| Number of pages | 7 |
| Journal | FEBS Letters |
| Volume | 579 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - Apr 25 2005 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology
Cite this
Effect of EPS1 gene deletion in Saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges. / He, Jianwei; Sakamoto, Takashi; Song, Youtao; Saito, Akira; Harada, Akihito; Azakami, Hiroyuki; Kato, Akio.
In: FEBS Letters, Vol. 579, No. 11, 25.04.2005, p. 2277-2283.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Effect of EPS1 gene deletion in Saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges
AU - He, Jianwei
AU - Sakamoto, Takashi
AU - Song, Youtao
AU - Saito, Akira
AU - Harada, Akihito
AU - Azakami, Hiroyuki
AU - Kato, Akio
PY - 2005/4/25
Y1 - 2005/4/25
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=17644364048&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=17644364048&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2005.03.019
DO - 10.1016/j.febslet.2005.03.019
M3 - Article
VL - 579
SP - 2277
EP - 2283
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 11
ER -