Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
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DOI：
10.1016/s1097-2765(00)80198-7
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发表时间：
1999-10-01
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
内质网（ER）中天然蛋白质二硫键的形成需要蛋白质二硫键异构酶（PDI）和Ero 1 p。在这里，我们表明，氧化当量流Ero 1 p通过PDI的底物蛋白质。PDI在野生型细胞中主要被氧化，但在ero 1 -1突变体中被还原。PDI和Ero 1 p之间的直接二硫醇-二硫键交换由PDI-Ero 1 p混合二硫键的捕获指示。还可以在PDI和羧肽酶Y（CPY）的ER前体之间检测到混合二硫化物。此外，PDI 1是新合成的CPY中二硫键的净形成所必需的，表明PDI在体内起氧化酶的作用。总之，这些结果定义了ER中蛋白质二硫键形成的途径。PDI同系物Mpd 2 p也被Ero 1 p氧化。
Native protein disulfide bond formation in the endoplasmic reticulum (ER) requires protein disulfide isomerase (PDI) and Ero1p. Here we show that oxidizing equivalents flow from Ero1p to substrate proteins via PDI. PDI is predominantly oxidized in wild-type cells but is reduced in an ero1-1 mutant. Direct dithiol-disulfide exchange between PDI and Ero1p is indicated by the capture of PDI-Ero1p mixed disulfides. Mixed disulfides can also be detected between PDI and the ER precursor of carboxypeptidase Y (CPY). Further, PDI1 is required for the net formation of disulfide bonds in newly synthesized CPY, indicating that PDI functions as an oxidase in vivo. Together, these results define a pathway for protein disulfide bond formation in the ER. The PDI homolog Mpd2p is also oxidized by Ero1p.