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二硫键蛋白质组和其他反应性半胱氨酸蛋白质组:分析与功能意义。

The disulfide proteome and other reactive cysteine proteomes: analysis and functional significance.

机构信息

Instituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas-Universidad de Sevilla, Centro de Investigaciones Científicas Isla de la Cartuja, Seville, Spain.

出版信息

Antioxid Redox Signal. 2011 Jun 15;14(12):2581-642. doi: 10.1089/ars.2010.3551. Epub 2011 Mar 31.

DOI:10.1089/ars.2010.3551
PMID:21275844
Abstract

Ten years ago, proteomics techniques designed for large-scale investigations of redox-sensitive proteins started to emerge. The proteomes, defined as sets of proteins containing reactive cysteines that undergo oxidative post-translational modifications, have had a particular impact on research concerning the redox regulation of cellular processes. These proteomes, which are hereafter termed "disulfide proteomes," have been studied in nearly all kingdoms of life, including animals, plants, fungi, and bacteria. Disulfide proteomics has been applied to the identification of proteins modified by reactive oxygen and nitrogen species under stress conditions. Other studies involving disulfide proteomics have addressed the functions of thioredoxins and glutaredoxins. Hence, there is a steadily growing number of proteins containing reactive cysteines, which are probable targets for redox regulation. The disulfide proteomes have provided evidence that entire pathways, such as glycolysis, the tricarboxylic acid cycle, and the Calvin-Benson cycle, are controlled by mechanisms involving changes in the cysteine redox state of each enzyme implicated. Synthesis and degradation of proteins are processes highly represented in disulfide proteomes and additional biochemical data have established some mechanisms for their redox regulation. Thus, combined with biochemistry and genetics, disulfide proteomics has a significant potential to contribute to new discoveries on redox regulation and signaling.

摘要

十年前,用于大规模研究氧化还原敏感蛋白的蛋白质组学技术开始出现。蛋白质组被定义为包含易发生氧化翻译后修饰的反应性半胱氨酸的蛋白质组,对研究细胞过程的氧化还原调控产生了特殊影响。这些蛋白质组,此后被称为“二硫键蛋白质组”,已经在几乎所有生命领域进行了研究,包括动物、植物、真菌和细菌。二硫键蛋白质组学已被应用于鉴定应激条件下由活性氧和氮物种修饰的蛋白质。其他涉及二硫键蛋白质组学的研究涉及硫氧还蛋白和谷氧还蛋白的功能。因此,越来越多的含有反应性半胱氨酸的蛋白质被确定为可能的氧化还原调控靶点。二硫键蛋白质组学提供了证据表明,整个途径,如糖酵解、三羧酸循环和卡尔文-本森循环,都受到涉及每个涉及的酶的半胱氨酸氧化还原状态变化的机制的控制。蛋白质的合成和降解是二硫键蛋白质组中高度代表性的过程,并且额外的生化数据已经建立了它们的氧化还原调控的一些机制。因此,与生物化学和遗传学相结合,二硫键蛋白质组学在氧化还原调控和信号转导方面的新发现方面具有很大的潜力。

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