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首页> 外文期刊>Journal of Molecular Biology >Structural analysis of cysteine S-nitrosylation: a modified acid-based motif and the emerging role of trans-nitrosylation.
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Structural analysis of cysteine S-nitrosylation: a modified acid-based motif and the emerging role of trans-nitrosylation.

机译：半胱氨酸S-亚硝基化的结构分析：修饰的基于酸的基序和反式亚硝基化的新兴作用。

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摘要

S-Nitrosylation, the selective and reversible addition of nitric oxide (NO) moiety to cysteine (Cys) sulfur in proteins, regulates numerous cellular processes. In recent years, proteomic approaches that are capable of identifying nitrosylated Cys residues have been developed. However, the features underlying the specificity of Cys modification with NO remain poorly defined. Previous studies suggested that S-nitrosylated Cys may be flanked by an acid-base motif or hydrophobic areas and show high reactivity, low pK(a), and high sulfur atom exposure. In the current study, we prepared an extensive, manually curated data set of proteins with S-nitrosothiols, accounting for a variety of biochemical functions, organisms of origin, and physiological responses to NO. Analysis of this generic NO-Cys data set revealed that proximal acid-base motif, Cys pK(a), sulfur atom exposure, and Cys conservation or hydrophobicity in the vicinity of the modified Cys do not define the specificity of S-nitrosylation. Instead, this analysis revealed a revised acid-base motif, which is located more distantly to the Cys and has its charged groups exposed. We hypothesize that, rather than being strictly used for direct activation of Cys, the modified acid-base motif is engaged in protein-protein interactions thereby contributing to trans-nitrosylation as an important and widespread mechanism for reversible modification of Cys with NO moiety. For proteins lacking the revised motif, we discuss alternative mechanisms including a potential role of nitrosoglutathione as a trans-acting agent.
机译：S-亚硝基化是蛋白质中半胱氨酸（Cys）硫选择性和可逆地添加的一氧化氮（NO）部分，可调节许多细胞过程。近年来，已经开发了能够鉴定亚硝基化的Cys残基的蛋白质组学方法。但是，用NO修饰Cys的特异性的潜在特征仍然定义不清。先前的研究表明，S-亚硝基化的Cys可能侧接酸碱基序或疏水区域，并显示出高反应活性，低pK（a）和高硫原子暴露量。在当前的研究中，我们准备了具有S-亚硝基硫醇的蛋白质的大量人工数据集，这些数据集说明了多种生化功能，起源生物以及对NO的生理反应。对该通用NO-Cys数据集的分析表明，近端酸基基序，Cys pK（a），硫原子暴露以及修饰的Cys附近的Cys保守性或疏水性并未定义S-亚硝基化的特异性。相反，该分析揭示了修正的酸碱基序，该基序与Cys距离更远，并且其带电基团暴露在外。我们假设，不是严格地用于Cys的直接激活，而是修饰的酸碱基序参与了蛋白质-蛋白质相互作用，从而促进了亚硝基化反应，将其作为重要且广泛的机制，对Cys进行NO部分的可逆修饰。对于缺少修饰基序的蛋白质，我们讨论了其他机制，包括亚硝基谷胱甘肽作为反式作用剂的潜在作用。

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