The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
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DOI：
10.1016/s1097-2765(00)80017-9
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发表时间：
1998-01-01
期刊：
影响因子：
16
通讯作者：
Kaiser, CA
中科院分区：
文献类型：
--
作者：
Frand, AR;Kaiser, CA
我们描述了一个保守的酵母基因ERO1，它由未折叠的蛋白质反应诱导，并编码内质网中氧化蛋白质折叠所需的一种新的糖蛋白。在对温度敏感的ero1-1突变体中，新合成的羧基肽酶Y保留在内质网中，并且没有二硫键，AMS对硫醇的修饰表明。ERO1显然决定了细胞的氧化能力，因为ERO1的突变导致了对还原剂DTT的过敏，而ERO1的过度表达则赋予了对DTT的抵抗力。此外，氧化剂联胺还可以恢复ero1突变体的生长和分泌。基因测试区分ERO1和PDI1的基本功能。我们证明了谷胱甘肽不是cpy折叠所必需的，并得出结论，Ero1p以一种新的机制发挥作用，该机制维持ER氧化电位，支持蛋白质二硫键的净形成。
We describe a conserved yeast gene, ERO1, that is induced by the unfolded protein response and encodes a novel glycoprotein required for oxidative protein folding in the ER. In a temperature-sensitive ero1-1 mutant, newly synthesized carboxypeptidase Y is retained in the ER and lacks disulfide bonds, as shown by thiol modification with AMS. ERO1 apparently determines cellular oxidizing capacity since mutation of ERO1 causes hypersensitivity to the reductant DTT, whereas overexpression of ERO1 confers resistance to DTT. Moreover, the oxidant diamide can restore growth and secretion in ero1 mutants. Genetic tests distinguish the essential function of ERO1 from that of PDI1. We show that glutathione is not required for CPY folding and conclude that Ero1p functions in a novel mechanism that sustains the ER oxidizing potential, supporting net formation of protein disulfide bonds.