大肠杆菌 DsbC 蛋白在抗氧化应激中的新作用。
A new role for Escherichia coli DsbC protein in protection against oxidative stress.
机构信息
From the de Duve Institute, Université catholique de Louvain, 1200 Brussels, Belgium.
出版信息
J Biol Chem. 2014 May 2;289(18):12356-64. doi: 10.1074/jbc.M114.554055. Epub 2014 Mar 14.
Abstract
We report a new function for Escherichia coli DsbC, a protein best known for disulfide bond isomerization in the periplasm. We found that DsbC regulates the redox state of the single cysteine of the L-arabinose-binding protein AraF. This cysteine, which can be oxidized to a sulfenic acid, mediates the formation of a disulfide-linked homodimer under oxidative stress conditions, preventing L-arabinose binding. DsbC, unlike the homologous protein DsbG, reduces the intermolecular disulfide, restoring AraF binding properties. Thus, our results reveal a new link between oxidative protein folding and the defense mechanisms against oxidative stress.
摘要
我们报告了大肠杆菌 DsbC 的一个新功能，该蛋白最著名的功能是在周质中进行二硫键异构化。我们发现 DsbC 调节 L-阿拉伯糖结合蛋白 AraF 的单个半胱氨酸的氧化还原状态。该半胱氨酸可以被氧化为亚磺酸，在氧化应激条件下形成二硫键连接的同源二聚体，从而阻止 L-阿拉伯糖结合。与同源蛋白 DsbG 不同，DsbC 还原分子间二硫键，恢复 AraF 的结合特性。因此，我们的结果揭示了氧化蛋白折叠和抗氧化应激防御机制之间的新联系。
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