Nitric oxide-based protein modification: formation and site-specificity of protein S-nitrosylation.
Nitric oxide-based protein modification: formation and site-specificity of protein S-nitrosylation.
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DOI：
10.3389/fpls.2013.00137
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发表时间：
2013
影响因子：
5.6
通讯作者：
Lindermayr C
中科院分区：
文献类型：
--
作者：
Kovacs I;Lindermayr C
一氧化氮（NO）是一种具有多效性的活性自由基，参与植物的多种生物学过程，如萌发、根的发育、气孔关闭、非生物胁迫和防御反应等。NO主要通过对靶蛋白的半胱氨酸残基进行氧化还原修饰（蛋白质S-亚硝基化）来发挥作用，从而调节植物细胞的多种功能和信号转导。确定S-亚硝基化底物及其准确的靶半胱氨酸残基对于揭示S-亚硝基化的分子机制和调控作用具有重要意义。除了蛋白质-蛋白质相互作用对转亚硝基化和去亚硝基化反应的必要性外，细胞氧化还原环境和半胱氨酸巯基微环境已被提出是蛋白质S-亚硝基化特异性的重要因素。最近已经开发了几种用于靶蛋白的蛋白质组学鉴定的方法。然而，基于NO的半胱氨酸修饰的特异性仍然不太确定。本文综述了S-亚硝基化的形成和特异性。特别关注的是潜在的S-亚硝基基序，位点特异性蛋白质组学分析，使用不同算法的计算预测，以及半胱氨酸S-亚硝基化的结构分析。
Nitric oxide (NO) is a reactive free radical with pleiotropic functions that participates in diverse biological processes in plants, such as germination, root development, stomatal closing, abiotic stress, and defense responses. It acts mainly through redox-based modification of cysteine residue(s) of target proteins, called protein S-nitrosylation.In this way NO regulates numerous cellular functions and signaling events in plants. Identification of S-nitrosylated substrates and their exact target cysteine residue(s) is very important to reveal the molecular mechanisms and regulatory roles of S-nitrosylation. In addition to the necessity of protein–protein interaction for trans-nitrosylation and denitrosylation reactions, the cellular redox environment and cysteine thiol micro-environment have been proposed important factors for the specificity of protein S-nitrosylation. Several methods have recently been developed for the proteomic identification of target proteins. However, the specificity of NO-based cysteine modification is still less defined. In this review, we discuss formation and specificity of S-nitrosylation. Special focus will be on potential S-nitrosylation motifs, site-specific proteomic analyses, computational predictions using different algorithms, and on structural analysis of cysteine S-nitrosylation.
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