National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
Genes Dev. 2010 Sep 1;24(17):1876-81. doi: 10.1101/gad.1956010. Epub 2010 Aug 16.
Piwi proteins are modified by symmetric dimethylation of arginine (sDMA), and the methylarginine-dependent interaction with Tudor domain proteins is critical for their functions in germline development. Cocrystal structures of an extended Tudor domain (eTud) of Drosophila Tudor with methylated peptides of Aubergine, a Piwi family protein, reveal that sDMA is recognized by an asparagine-gated aromatic cage. Furthermore, the unexpected Tudor-SN/p100 fold of eTud is important for sensing the position of sDMA. The structural information provides mechanistic insights into sDMA-dependent Piwi-Tudor interaction, and the recognition of sDMA by Tudor domains in general.
Piwi 蛋白通过精氨酸的对称二甲基化(sDMA)修饰,甲基化精氨酸与 Tudor 结构域蛋白的相互作用对于它们在生殖细胞发育中的功能至关重要。果蝇 Tudor 延长结构域(eTud)与 Piwi 家族蛋白 Aubergine 的甲基化肽的共晶结构揭示了 sDMA 被天门冬酰胺门控芳香笼识别。此外,eTud 的意想不到的 Tudor-SN/p100 折叠对于感知 sDMA 的位置很重要。结构信息为 sDMA 依赖性 Piwi-Tudor 相互作用以及一般情况下 Tudor 结构域识别 sDMA 提供了机制见解。