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pubmed-article:15848158pubmed:abstractTextBoth amyloid-prone cystatin and unstable mutant C94A lysozyme were secreted in wild-type and Deltaeps1 Saccharomyces cerevisiae cells. Amyloid-prone cystatin secreted at much higher level in Deltaeps1 cells than that in wild-type yeast. In parallel, the secretion amount of disulfide bond disrupted mutant C94A lysozyme greatly increased in Deltaeps1 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 Deltaeps1 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.lld:pubmed
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pubmed-article:15848158pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15848158pubmed:articleTitleEffect of EPS1 gene deletion in Saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges.lld:pubmed
pubmed-article:15848158pubmed:affiliationDepartment of Biological Chemistry, Yamaguchi University, Japan.lld:pubmed
pubmed-article:15848158pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15848158pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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