Structural basis for methylarginine-dependent recognition of Aubergine by Tudor

  1. Rui-Ming Xu1,8
  1. 1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China;
  2. 2Graduate University of Chinese Academy of Sciences, Beijing 100049, People's Republic of China;
  3. 3The Helen L. and Martin S. Kimmel Center for Biology and Medicine, Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, New York 10016, USA;
  4. 4Howard Hughes Medical Institute, New York University School of Medicine, New York, New York 10016, USA;
  5. 5Department of Cell Biology, New York University School of Medicine, New York, New York 10016, USA
    • 7 Present address: Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, People's Republic of China.

    1. 6 These authors contributed equally to this work.

    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

    Footnotes

    • Received June 3, 2010.
    • Accepted July 13, 2010.

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