Liu, H., Wang, J.Y., Huang, Y., Li, Z., Gong, W., Lehmann, R., Xu, R.M. (2010). Structural basis for methylarginine-dependent recognition of Aubergine by Tudor. Genes Dev. 24(17): 1876--1881.
FlyBase ID
FBrf0211676
Publication Type
Research paper
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.
