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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli
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Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli

机译：大肠杆菌中硫氧还蛋白靶向蛋白的蛋白质组学分析

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摘要

Thioredoxin, a ubiquitous and evolutionarily conserved protein, modulates the structure and activity of proteins involved in a spectrum of processes, such as gene expression, apoptosis, and the oxidative stress response. Here, we present a comprehensive analysis of the thioredoxin-linked Escherichia coli proteome by using tandem affinity purification and nanospray microcapillary tandem mass spectrometry. We have identified a total of 80 proteins associated with thioredoxin, implicating the involvement of thioredoxin in at least 26 distinct cellular processes that include transcription regulation, cell division, energy transduction, and several biosynthetic pathways. We also found a number of proteins associated with thioredoxin that either participate directly (SodA, HPI, and AhpC) or have key regulatory functions (Fur and AcnB) in the detoxification of the cell. Transcription factors NusG, OmpR, and RcsB, not considered to be under redox control, are also associated with thioredoxin. [References: 52]
机译：硫氧还蛋白是一种普遍存在且在进化上保守的蛋白质，可调节涉及一系列过程的蛋白质的结构和活性，这些过程包括基因表达，细胞凋亡和氧化应激反应。在这里，我们提出了通过使用串联亲和纯化和纳米喷雾微毛细管串联质谱对硫氧还蛋白连接的大肠杆菌蛋白质组的全面分析。我们已经鉴定出总共80种与硫氧还蛋白相关的蛋白质，这意味着硫氧还蛋白参与了至少26种不同的细胞过程，这些过程包括转录调控，细胞分裂，能量转导和几种生物合成途径。我们还发现了许多与硫氧还蛋白相关的蛋白质，它们在细胞排毒中直接参与（SodA，HPI和AhpC）或具有关键调控功能（Fur和AcnB）。转录因子NusG，OmpR和RcsB（未被认为受氧化还原控制）也与硫氧还蛋白有关。 [参考：52]

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