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首页> 外文期刊>Antioxidants and redox signalling >Thioredoxin 1-mediated post-translational modifications: reduction, transnitrosylation, denitrosylation, and related proteomics methodologies.
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Thioredoxin 1-mediated post-translational modifications: reduction, transnitrosylation, denitrosylation, and related proteomics methodologies.

机译：硫氧还蛋白1介导的翻译后修饰：还原，反式亚硝基化，反式亚硝基化和相关的蛋白质组学方法。

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摘要

Despite the significance of redox post-translational modifications (PTMs) in regulating diverse signal transduction pathways, the enzymatic systems that catalyze reversible and specific oxidative or reductive modifications have yet to be firmly established. Thioredoxin 1 (Trx1) is a conserved antioxidant protein that is well known for its disulfide reductase activity. Interestingly, Trx1 is also able to transnitrosylate or denitrosylate (defined as processes to transfer or remove a nitric oxide entity to/from substrates) specific proteins. An intricate redox regulatory mechanism has recently been uncovered that accounts for the ability of Trx1 to catalyze these different redox PTMs. In this review, we will summarize the available evidence in support of Trx1 as a specific disulfide reductase, and denitrosylation and transnitrosylation agent, as well as the biological significance of the diverse array of Trx1-regulated pathways and processes under different physiological contexts. The dramatic progress in redox proteomics techniques has enabled the identification of an increasing number of proteins, including peroxiredoxin 1, whose disulfide bond formation and nitrosylation status are regulated by Trx1. This review will also summarize the advancements of redox proteomics techniques for the identification of the protein targets of Trx1-mediated PTMs. Collectively, these studies have shed light on the mechanisms that regulate Trx1-mediated reduction, transnitrosylation, and denitrosylation of specific target proteins, solidifying the role of Trx1 as a master regulator of redox signal transduction.
机译：尽管氧化还原后翻译修饰（PTM）在调节各种信号转导途径中具有重要意义，但催化体系可逆和特定的氧化或还原修饰的酶体系尚未得到牢固确立。硫氧还蛋白1（Trx1）是一种保守的抗氧化剂蛋白，因其二硫键还原酶活性而闻名。有趣的是，Trx1还能够反硝化或脱亚硝基化（定义为将一氧化氮实体转移至底物或从底物中去除一氧化氮的过程）。最近发现了一种复杂的氧化还原调节机制，该机制解释了Trx1催化这些不同的氧化还原PTM的能力。在这篇综述中，我们将总结支持Trx1作为特定的二硫键还原酶，脱亚硝基化和反硝化试剂的现有证据，以及在不同生理环境下Trx1调控的各种途径和过程的生物学意义。氧化还原蛋白质组学技术的巨大进步使人们能够鉴定出越来越多的蛋白质，包括过氧化物酶1，其二硫键形成和亚硝基化状态受Trx1调控。这篇综述还将总结氧化还原蛋白质组学技术在Trx1介导的PTMs蛋白质靶标鉴定中的进展。总的来说，这些研究阐明了调节Trx1介导的特定靶蛋白还原，反硝化和脱亚硝化的机制，巩固了Trx1作为氧化还原信号转导的主要调节剂的作用。

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