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Effect of EPS1 gene deletion in Saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges
Author(s) -
He Jianwei,
Sakamoto Takashi,
Song Youtao,
Saito Akira,
Harada Akihito,
Azakami Hiroyuki,
Kato Akio
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.019
Subject(s) - lysozyme , secretion , protein disulfide isomerase , saccharomyces cerevisiae , mutant , yeast , secretory protein , biochemistry , chemistry , cysteine , cystatin , wild type , secretory pathway , cystatin c , microbiology and biotechnology , biology , gene , enzyme , endoplasmic reticulum , renal function , golgi apparatus
Both amyloid‐prone cystatin and unstable mutant C94A lysozyme were secreted in wild‐type and Δ eps 1 Saccharomyces cerevisiae cells. Amyloid‐prone cystatin secreted at much higher level in Δ eps 1 cells than that in wild‐type yeast. In parallel, the secretion amount of disulfide bond disrupted mutant C94A lysozyme greatly increased in Δ eps 1 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 Δ eps 1 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.