Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae.

Rmt1 catalyzes zinc-finger independent arginine methylation of ribosomal protein Rps2 in Saccharomyces cerevisiae.
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DOI:
10.1016/j.bbrc.2009.12.112
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发表时间:
2010-01-22
影响因子:
3.1
通讯作者:
Clarke, Steven G.
Clarke, Steven G.
中科院分区:
生物学4区
文献类型:
--
作者:
Lipson, Rebecca S.;Webb, Kristofor J.;Clarke, Steven G.

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Rps 2/rpS 2是真核生物核糖体小亚基中高度保守的蛋白质。Rps 2先前已被证明含有不对称二甲基精氨酸残基,其添加由裂殖酵母裂殖酵母中的含锌指精氨酸甲基转移酶3(Rmt 3)和哺乳动物细胞中的蛋白质精氨酸甲基转移酶3(PRMT 3)催化。在这里,我们表明,尽管缺乏含锌指的同源物的RMT 3/PRMT 3在芽殖酵母酿酒酵母,RPS 2部分修改,产生不对称的二甲基精氨酸和单甲基精氨酸残基。我们发现Rps 2的这种修饰依赖于S中主要的精氨酸甲基转移酶1(Rmt 1)。啤酒。这些结果提示Rmt 1以不同于S中发生的方式在修饰Rps 2的功能中的作用。粟酒酵母和哺乳动物细胞。
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.
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