Structural basis for methylarginine-dependent recognition of Aubergine by Tudor
- 16 August 2010
- journal article
- research article
- Published by Cold Spring Harbor Laboratory in Genes & Development
- Vol. 24 (17), 1876-1881
- https://doi.org/10.1101/gad.1956010
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.Keywords
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