Camerini Serena, Polci Maria L, Restuccia Umberto, Usuelli Vera, Malgaroli Antonio, Bachi Angela
San Raffaele Scientific Institute, 20132 Milan, Italy.
J Proteome Res. 2007 Aug;6(8):3224-31. doi: 10.1021/pr0701456. Epub 2007 Jul 13.
S-nitrosylation is emerging as an important signaling mechanism that regulates a broad range of cellular functions. The recognition of Cysteine residues that undergo S-nitrosylation is crucial to elucidate how this modification modulates protein activity. We report here a novel strategy, defined His-tag switch, which allows the purification and identification of S-nitrosylated proteins and the unambiguous localization of the modified cysteine residues by mass spectrometry analysis.
S-亚硝基化正成为一种重要的信号传导机制,可调节广泛的细胞功能。识别发生S-亚硝基化的半胱氨酸残基对于阐明这种修饰如何调节蛋白质活性至关重要。我们在此报告一种新策略,即定义的His标签转换,它允许通过质谱分析纯化和鉴定S-亚硝基化蛋白以及明确修饰的半胱氨酸残基的定位。