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用于鉴定 S-亚硝基化蛋白质的筛选系统。

Screening systems for the identification of S-nitrosylated proteins.

机构信息

Department of Medicinal Pharmacology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama 700-8530, Japan.

出版信息

Nitric Oxide. 2011 Aug 1;25(2):108-11. doi: 10.1016/j.niox.2010.11.002. Epub 2010 Nov 24.

DOI:10.1016/j.niox.2010.11.002
PMID:21111056
Abstract

S-nitrosylation is a well-characterized reaction involving the covalent binding of nitric oxide (NO) to cysteine residues (Cys) in a protein. Similar to protein phosphorylation, S-nitrosylation is a post-translational modification involved in the regulation of a large number of intracellular functions and signaling events. Moreover, like phosphorylation, S-nitrosylation is precisely regulated in time and space. A procedure known as the biotin-switch method that specifically detects S-nitrosylated proteins (SNO-P) was recently developed by Snyder's group. They found that many proteins are substrates for NO, and several groups have attempted to identify other SNO-P by improving this method. In this review, we describe the SNO-P identified using modified versions of the biotin-switch method.

摘要

S-亚硝基化是一种经过充分研究的反应,涉及将一氧化氮 (NO) 共价结合到蛋白质中的半胱氨酸残基 (Cys) 上。与蛋白质磷酸化类似,S-亚硝基化是一种参与调节大量细胞内功能和信号事件的翻译后修饰。此外,与磷酸化一样,S-亚硝基化在时间和空间上受到精确调节。Snyder 小组最近开发了一种称为生物素开关方法的程序,该方法专门检测 S-亚硝基化蛋白质 (SNO-P)。他们发现许多蛋白质都是 NO 的底物,并且有几个小组试图通过改进该方法来鉴定其他 SNO-P。在这篇综述中,我们描述了使用生物素开关方法的修改版本鉴定的 SNO-P。

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