Oxidative protein folding: selective pressure for prolamin evolution in rice.
Oxidative protein folding: selective pressure for prolamin evolution in rice.
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DOI：
10.4161/psb.6.12.17967
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发表时间：
2011-12
影响因子：
2.9
通讯作者：
Kawagoe Y
中科院分区：
文献类型：
--
作者：
Onda Y;Kawagoe Y
在种子发育过程中，高产谷物（包括水稻）的胚乳细胞大量合成富含二硫化物的蛋白质，并将其存款到储存细胞器中。二硫键的形成涉及电子转移并产生H2O2作为副产物。为了确保种子的正常发育和成熟，胚乳细胞必须以受控的方式提供大量的氧化当量给新生蛋白质中的二硫醇。本文比较了酵母、培养的人类细胞和水稻胚乳中的多种氧化蛋白质折叠系统。我们讨论了ERO1，其他巯基氧化酶，和蛋白质二硫键异构酶家族中的二硫键的形成在存储蛋白质和蛋白体的发展可能发挥的作用。水稻醇溶蛋白是一个多基因家族，分为富含半胱氨酸和缺乏半胱氨酸两个亚类。我们讨论了二硫键的形成在粳稻醇溶蛋白家族进化中的潜在重要性。
During seed development, endosperm cells of highly productive cereals, including rice, synthesize disulfide-rich proteins in large amounts and deposit them into storage organelles. Disulfide bond formation involves electron transfer and generates H2O2 as a by-product. To ensure proper development and maturation of seeds, the endosperm cells must supply large amounts of oxidizing equivalents to dithiols in nascent proteins in a controlled manner. This review compares multiple oxidative protein folding systems in yeast, cultured human cells, and rice endosperm. We discuss possible roles of ERO1, other sulfhydryl oxidases, and the protein disulfide isomerase family in the formation of disulfide bonds in storage proteins and the development of protein bodies. Rice prolamins, encoded by a multigene family, are divided into Cys-rich and Cys-depleted subgroups. We discuss the potential importance of disulfide bond formation in the evolution of the prolamin family in japonica rice.