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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae
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All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae

机译:所有亲环蛋白和FK506结合蛋白对于酿酒酵母的生存力都是单独的和共同的

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摘要

The cyclophilins and FK506 binding proteins (FKBPs) bind to cyclosporin A, FK506, and rapamycin and mediate their immunosuppressive and toxic effects, but the phys- iological functions of these proteins are largely unknown. Cyclo- philins and FKBPs are ubiquitous and highly conserved enzymes that catalyze peptidyl-prolyl isomerization, a rate-limiting step during in vitro protein folding. We have addressed their functions by a genetic approach in the yeast Saccharomyces cerevisiae. Five cyclophilins and three FKBPs previously were identified in yeast.
机译:亲环蛋白和FK506结合蛋白(FKBPs)与环孢菌素A,FK506和雷帕霉素结合并介导其免疫抑制和毒性作用,但这些蛋白的生理功能尚不清楚。亲环素和FKBP是普遍存在且高度保守的酶,可催化肽基脯氨酰异构化,这是体外蛋白质折叠过程中的限速步骤。我们已经通过遗传方法在酿酒酵母中解决了它们的功能。以前在酵母中鉴定出五个亲环蛋白和三个FKBP。

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