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Title: Structural basis for methylarginine-dependent recognition of Aubergine by Tudor. Author: Liu H, Wang JY, Huang Y, Li Z, Gong W, Lehmann R, Xu RM. Journal: Genes Dev; 2010 Sep 01; 24(17):1876-81. PubMed ID: 20713507. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]