Cook Jeffry R, Lee Jin-Hyung, Yang Zhi-Hong, Krause Christopher D, Herth Nicole, Hoffmann Ralf, Pestka Sidney
UMDNJ-Robert Wood Johnson Medical School, Molecular Genetics and Immunology, 675 Hoes Lane, Rm 727, Piscataway, NJ 08854, USA.
Biochem Biophys Res Commun. 2006 Apr 7;342(2):472-81. doi: 10.1016/j.bbrc.2006.01.167. Epub 2006 Feb 8.
We have identified a protein, FLJ12673 or FBXO11, that contains domains characteristically present in protein arginine methyltransferases (PRMTs). Immuno-purified protein expressed from one of the four splice variants in HeLa cells and in Escherichia coli exhibited methyltransferase activity. Monomethylarginine, symmetric, and asymmetric dimethylarginine (SDMA, ADMA) were formed on arginine residues. Accordingly, we have designated the protein PRMT9. PRMT9 is the third member of the PRMT family that forms SDMA modifications in proteins. Structurally, this protein is distinct from all other known PRMTs implying that convergent evolution allowed this protein to develop the ability to methylate arginine residues and evolved elements conserved in PRMTs to accomplish this.
我们鉴定出一种蛋白质，即FLJ12673或FBXO11，它含有蛋白质精氨酸甲基转移酶（PRMT）中特有的结构域。从HeLa细胞和大肠杆菌中的四种剪接变体之一表达的免疫纯化蛋白表现出甲基转移酶活性。在精氨酸残基上形成了单甲基精氨酸、对称和不对称二甲基精氨酸（SDMA、ADMA）。因此，我们将该蛋白质命名为PRMT9。PRMT9是PRMT家族中第三个在蛋白质中形成SDMA修饰的成员。在结构上，这种蛋白质与所有其他已知的PRMT不同，这意味着趋同进化使该蛋白质发展出甲基化精氨酸残基的能力，并进化出PRMT中保守的元件来实现这一点。
