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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >ER membrane-localized oxidoreductase Ero1 is required for disulfide bond formation in the rice endosperm
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ER membrane-localized oxidoreductase Ero1 is required for disulfide bond formation in the rice endosperm

机译：水稻胚乳中二硫键形成需要ER膜局部氧化还原酶Ero1

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摘要

The developing endosperm of rice (Oryza sativa, Os) synthesizes a large amount of storage proteins on the rough (r)ER. The major storage proteins, glutelins and prolamins, contain either intra or intermolecular disulfide bonds, and oxidative protein folding is necessary for the sorting of the proteins to the protein bodies. Here, we investigated an electron transfer pathway for the formation of protein disulfide bonds in the rER of the rice endosperm, focusing on the roles of the thiol-disulfide oxidoreductase, OsEro1. Confocal microscopic analysis revealed that N-glycosylated OsEro1 is localized to the rER membrane in the subaleurone cells, and that targeting of OsEro1 to the rER membrane depends on the N-terminal region from Met-1 to Ser-55. The RNAi knockdown of OsERO1 inhibited the formation of native disulfide bonds in the glutelin precursors (pro-glutelins) and promoted aggregation of the proglutelins through nonnative intermolecular disulfide bonds in the rER. Inhibition of the formation of native disulfide bonds was also observed in the seeds of the esp2 mutant, which lacks protein disulfide isomerase-like (PDIL)1;1, but shows enhanced OsEro1 expression. We detected the generation of H_2O_2 in the rER of the WT subaleurone cells, whereas the rER-derived H_2O_2 levels decreased markedly in EM49 homozygous mutant seeds, which have fewer sulfhydryl groups than the WT seeds. Together, we propose that the formation of native disulfide bonds in proglutelins depends on an electron transfer pathwayrninvolving OsEro1 and OsPDIL.
机译：水稻（Oryza sativa，Os）的发育胚乳在粗糙的（r）ER上合成了大量的存储蛋白。主要的贮藏蛋白，谷蛋白和谷醇溶蛋白含有分子内或分子间的二硫键，氧化蛋白折叠对于将蛋白分选到蛋白体是必需的。在这里，我们研究了在稻胚乳的rER中形成蛋白质二硫键的电子转移途径，重点研究了巯基二硫键氧化还原酶OsEro1的作用。共聚焦显微镜分析显示，N-糖基化的OsEro1位于亚aleroneer细胞中的rER膜上，而OsEro1靶向rER膜则取决于从Met-1到Ser-55的N端区域。 OsERO1的RNAi抑制抑制了谷蛋白原（pro-glutelins）中天然二硫键的形成，并通过rER中的非天然分子间二硫键促进了proglutelins的聚集。 esp2突变体的种子中也观察到天然二硫键形成的抑制，该突变体缺少蛋白质二硫键异构酶样（PDIL）1; 1，但显示出增强的OsEro1表达。我们检测到WT亚alaloneer细胞的rER中H_2O_2的生成，而rER衍生的H_2O_2水平在EM49纯合突变体种子中显着降低，该种子具有比WT种子更少的巯基。在一起，我们建议在proglutelins中天然二硫键的形成取决于一个涉及OsEro1和OsPDIL的电子转移途径。

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