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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Balancing oxidative protein folding: The influences of reducing pathways on disulfide bond formation
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Balancing oxidative protein folding: The influences of reducing pathways on disulfide bond formation

机译：平衡氧化性蛋白质折叠：还原途径对二硫键形成的影响

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Oxidative protein folding is confined to few compartments, including the endoplasmic reticulum, the mitochondrial intermembrane space and the bacterial periplasm. Conversely, in compartments in which proteins are translated such as the cytosol, the mitochondrial matrix and the chloroplast stroma proteins are kept reduced by the thioredoxin and glutaredoxin systems that functionally overlap. The highly reducing NADPH pool thereby serves as electron donor that enables glutathione reductase and thioredoxin reductase to keep glutathione pools and thioredoxins in their reduced redox state, respectively. Notably, also compartments containing oxidizing machineries are linked to these reducing pathways. Reducing pathways aid in proofreading of disulfide bond formation by isomerization or they provide reducing equivalents for the reduction of disulfides prior to degradation. In addition, they contribute to the thiol-dependent regulation of protein activities, and they help to counteract oxidative stress. The existence of oxidizing and reducing pathways in the same compartment poses a potential problem as the cell has to avoid futile cycles of oxidation and subsequent reduction reactions. Thus, compartments that contain oxidizing machineries have developed sophisticated ways to spatiotemporally balance and regulate oxidation and reduction. In this review, we discuss oxidizing and reducing pathways in the endoplasmic reticulum, the periplasm and the mitochondrial intermembrane space and highlight the role of glutathione especially in the endoplasmic reticulum and the intermembrane space. This article is part of a Special Issue entitled: Thiol-Based Redox Processes.
机译：氧化性蛋白折叠被限制在几个小室中，包括内质网，线粒体膜间空间和细菌周质。相反，在其中翻译有诸如胞浆之类的蛋白质的隔室中，线粒体基质和叶绿体基质蛋白质被功能上重叠的硫氧还蛋白和戊二醛毒素系统保持还原。因此，高度还原的NADPH库充当电子供体，使谷胱甘肽还原酶和硫氧还蛋白还原酶分别将谷胱甘肽库和硫氧还蛋白保持在还原状态。值得注意的是，包含氧化机械的隔室也与这些还原途径相连。还原途径有助于通过异构化对二硫键形成的校对，或者它们提供了在降解前还原二硫化物的还原当量。此外，它们有助于蛋白质活性的硫醇依赖性调节，并且有助于抵消氧化应激。在同一隔室中存在氧化和还原途径构成了潜在的问题，因为电池必须避免徒劳的氧化循环和随后的还原反应。因此，包含氧化机械的隔室已经开发出复杂的方式来时空平衡并调节氧化和还原。在这篇综述中，我们讨论了内质网，周质和线粒体膜间空间中的氧化和还原途径，并突出了谷胱甘肽的作用，尤其是在内质网和膜间空间中的作用。本文是一个名为“基于硫醇的氧化还原过程”的特刊的一部分。

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