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KMID : 0545119990090020196
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Journal of Microbiology and Biotechnology
1999 Volume.9 No. 2 p.196 ~ p.200
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Secretory Expression of Human α_(s₁)-Casein in Saccharomyces cerevisiae
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Kim, Yoo Kyeong
Yu, Dae Yeul/Kang, Hyun Ah/Yoon, Sun/Chung, Bong Hyun
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Abstract
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A recombinant human α_1-casein was expressed as a secretory product in the yeast Saccharomvces cerevisiae. Three different leader sequences derived from the mating factor αl (MFαl), inulinase. and human α_1-casein were used to direct the secretion of human α_1-casein into the extracellular medium. Among the three leader sequences tested, the native leader sequence of human α_1-casein was found to he the most efficient in the secretory expression of human α_1-casein, which implies that the native leader sequence of human α_1-casein might be used very efficiently for the secretory production of other heterologous proteins in yeast. The recombinant human α_1-casein was proteolytically cleaved as the culture proceeded. Therefore, an attempt was made to produce human α_1-casein using a S. cerevisiae mutant in which the YAP3 gene encoding yeast aspartic protease 3 (YAPS) was disrupted. After 72 h of culture, most of the human α_1-casein secreted by the wild type was cleaved. whereas more than 70% of the human α_1-casein secreted by yap3-disruptant remained intact. The results suggest that YAP3 might he involved in the internal cleavage of human α_1-casein expressed in yeast
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