Department of Chemistry and Biochemistry and the Molecular Biology Institute, UCLA, 607 Charles E Young Drive East, Los Angeles, CA 90095-1569, USA.
Biochem Biophys Res Commun. 2010 Jan 22;391(4):1658-62. doi: 10.1016/j.bbrc.2009.12.112. Epub 2009 Dec 24.
Rps2/rpS2 is a well conserved protein of the eukaryotic ribosomal small subunit. Rps2 has previously been shown to contain asymmetric dimethylarginine residues, the addition of which is catalyzed by zinc-finger-containing arginine methyltransferase 3 (Rmt3) in the fission yeast Schizosaccharomyces pombe and protein arginine methyltransferase 3 (PRMT3) in mammalian cells. Here, we demonstrate that despite the lack of a zinc-finger-containing homolog of Rmt3/PRMT3 in the budding yeast Saccharomyces cerevisiae, Rps2 is partially modified to generate asymmetric dimethylarginine and monomethylarginine residues. We find that this modification of Rps2 is dependent upon the major arginine methyltransferase 1 (Rmt1) in S. cerevisiae. These results are suggestive of a role for Rmt1 in modifying the function of Rps2 in a manner distinct from that occurring in S. pombe and mammalian cells.
Rps2/rpS2 是真核核糖体小亚基中高度保守的蛋白质。先前的研究表明,Rps2 含有不对称二甲基精氨酸残基,该残基的添加由裂殖酵母 Schizosaccharomyces pombe 中的含锌指的精氨酸甲基转移酶 3(Rmt3)和哺乳动物细胞中的蛋白精氨酸甲基转移酶 3(PRMT3)催化。在这里,我们证明尽管酿酒酵母 Saccharomyces cerevisiae 中缺乏含锌指的 Rmt3/PRMT3 同源物,但 Rps2 会被部分修饰以生成不对称二甲基精氨酸和单甲基精氨酸残基。我们发现,Rps2 的这种修饰依赖于 S. cerevisiae 中的主要精氨酸甲基转移酶 1(Rmt1)。这些结果表明,Rmt1 可能在以不同于 S. pombe 和哺乳动物细胞的方式修饰 Rps2 的功能方面发挥作用。