The C. elegans PRMT-3 possesses a type III protein arginine methyltransferase activity
The C. elegans PRMT-3 possesses a type III protein arginine methyltransferase activity
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DOI：
10.3109/10799893.2011.555768
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发表时间：
2011-04-01
影响因子：
2.8
通讯作者：
Fukamizu, Akiyoshi
中科院分区：
文献类型：
--
作者：
Takahashi, Yuta;Daitoku, Hiroaki;Fukamizu, Akiyoshi
蛋白质精氨酸甲基化是真核生物中常见的翻译后修饰，由蛋白质精氨酸甲基转移酶（PRMT）家族催化。PRMT分为三种类型：I型和II型分别在精氨酸上不对称和对称地添加二甲基基团，而III型仅在精氨酸上添加单甲基基团。然而，尽管已经报道了I型和II型PRMT的酶活性，但III型PRMT的底物特异性和甲基化活性仍然未知。在这里，我们报告的特征秀丽隐杆线虫PRMT-2和PRMT-3，这两者都是高度同源的人PRMT 7。我们发现，这两个PRMT可以结合S-腺苷甲硫氨酸（SAM），但只有PRMT-3组蛋白H2 A依赖于其SAM结合结构域的甲基转移酶活性。重要的是，薄层色谱分析表明PRMT-3催化单甲基化而非二甲基化精氨酸的形成。因此，我们的研究确定了第一个III型PRMT在C。并提供了一种手段来阐明精氨酸单甲基化在多细胞生物中的生理意义。
Protein arginine methylation is a common post-translational modification in eukaryotes that is catalyzed by a family of the protein arginine methyltransferases (PRMTs). PRMTs are classified into three types: type I and type II add asymmetrically and symmetrically dimethyl groups to arginine, respectively, while type III adds solely monomethyl group to arginine. However, although the enzymatic activity of type I and type II PRMTs have been reported, the substrate specificity and the methylation activity of type III PRMTs still remains unknown. Here, we report the characterization of Caenorhabditis elegans PRMT-2 and PRMT-3, both of which are highly homologous to human PRMT7. We find that these two PRMTs can bind to S-adenosyl methionine (SAM), but only PRMT-3 has methyltransferase activity for histone H2A depending on its SAM-binding domain. Importantly, thin-layer chromatographic analysis demonstrates that PRMT-3 catalyzes the formation of monomethylated, but not dimethylated arginine. Our study thus identifies the first type III PRMT in C. elegans and provides a means to elucidate the physiological significance of arginine monomethylation in multicellular organisms.