Tudor domains bind symmetrical dimethylated arginines
Tudor domains bind symmetrical dimethylated arginines
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DOI：
10.1074/jbc.m414328200
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发表时间：
2005-08-05
影响因子：
4.8
通讯作者：
Richard, S
中科院分区：
文献类型：
--
作者：
Côté, J;Richard, S
Tudor结构域是一个类似于60个氨基酸的结构基序，用于寻找功能。在这里，我们表明，Tudor结构域的脊髓性肌萎缩症基因产物SMN，剪接因子30 kDa（SPF 30），和Tudor结构域包含3（TDRD 3）蛋白相互作用与精氨酸-甘氨酸丰富的图案在甲基精氨酸依赖的方式。Tudor结构域还与含甲基精氨酸的细胞蛋白相关，提供了甲基化精氨酸代表该蛋白模块的生理配体的证据。此外，我们报告说，剪接体小核核糖核蛋白颗粒核心Sm蛋白积累在细胞质中时，精氨酸甲基化被抑制与腺苷二醛或在存在过量的未甲基化的甘氨酸-甘氨酸丰富的肽。这些数据提供了体内证据，支持精氨酸甲基化在剪接体Sm蛋白的正确组装和定位中的作用。
The Tudor domain is an similar to 60-amino acid structure motif in search of a function. Herein we show that the Tudor domains of the spinal muscular atrophy gene product SMN, the splicing factor 30 kDa ( SPF30), and the Tudor domain-containing 3 ( TDRD3) proteins interacted with arginine-glycine-rich motifs in a methylarginine-dependent manner. The Tudor domains also associated with methylarginine-containing cellular proteins, providing evidence that methylated arginines represent physiological ligands for this protein module. In addition, we report that spliceosomal small nuclear ribonucleoprotein particles core Sm proteins accumulated in the cytoplasm when arginine methylation was inhibited with adenosine dialdehyde or in the presence of an excessive amount of unmethylated arginine-glycine-rich peptides. These data provide in vivo evidence in support of a role for arginine methylation in the proper assembly and localization of spliceosomal Sm proteins.