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首页> 外文期刊>The protein journal >Direct Mass-Spectrometric Identification of Arg296 and Arg299 as the Methylation Sites of hnRNP K Protein for Methyltransferase PRMT1.
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Direct Mass-Spectrometric Identification of Arg296 and Arg299 as the Methylation Sites of hnRNP K Protein for Methyltransferase PRMT1.

机译：直接质谱鉴定Arg296和Arg299作为甲基转移酶PRMT1的hnRNP K蛋白的甲基化位点。

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摘要

Protein methylation is one of the most important post-translational modifications that contribute to the diversity and complexity of proteome. Here we report the study of in vitro methylation of heterogeneous nuclear ribonucleoprotein K (hnRNP K) with protein arginine methyltransferase 1 (PRMT1), as an enzyme, and S-adenosyl-L: -methionine (SAM), as a methyl donor. The mass analysis of tryptic peptides of hnRNP K before and after methylation reveals the addition of four methyl groups in the residues 288-303. Tandem mass-spectrometric analysis of this peptide shows that both Arg296 and Arg299 are dimethylated. In addition, fragmentation analysis of such methylated arginines illustrate that they are both asymmetric dimethylarginines. Since Arg296 and Arg299 are located near the SH3-binding domains of hnRNP K, such methylation has the potential in regulating the interaction of hnRNP K with Src protein family. Our results provide crucial information for further functional study of hnRNP K methylation.
机译：蛋白质甲基化是导致蛋白质组多样性和复杂性的最重要的翻译后修饰之一。在这里，我们报告的研究与蛋白质精氨酸甲基转移酶1（PRMT1），作为一种酶和S-腺苷-L：-蛋氨酸（SAM），作为一个甲基供体的异质核糖核蛋白K（hnRNP K）的体外甲基化研究。甲基化之前和之后hnRNP K的胰蛋白酶肽的质量分析表明，在残基288-303中添加了四个甲基。对该肽的串联质谱分析显示，Arg296和Arg299均被二甲基化。另外，这种甲基化精氨酸的片段化分析表明它们都是不对称的二甲基精氨酸。由于Arg296和Arg299位于hnRNP K的SH3结合结构域附近，因此这种甲基化具有调节hnRNP K与Src蛋白家族相互作用的潜力。我们的结果为进一步研究hnRNP K甲基化提供了重要信息。

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