Structural basis for methylarginine-dependent recognition of Aubergine by Tudor
- Haiping Liu1,2,6,
- Ju-Yu S. Wang3,6,
- Ying Huang3,6,7,
- Zhizhong Li3,
- Weimin Gong1,
- Ruth Lehmann3,4,5,9 and
- Rui-Ming Xu1,8
- 1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China;
- 2Graduate University of Chinese Academy of Sciences, Beijing 100049, People's Republic of China;
- 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;
- 4Howard Hughes Medical Institute, New York University School of Medicine, New York, New York 10016, USA;
- 5Department of Cell Biology, New York University School of Medicine, New York, New York 10016, USA
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↵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.
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Footnotes
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↵8 Corresponding authors.
E-MAIL rmxu{at}sun5.ibp.ac.cn; FAX 86-10-648888023.
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↵9 E-MAIL lehmann{at}saturn.med.nyu.edu; FAX (212) 263-0614.
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Article published online ahead of print. Article and publication date are online at http://www.genesdev.org/cgi/doi/10.1101/gad.1956010.
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Supplemental material is available at http://www.genesdev.org.
- Received June 3, 2010.
- Accepted July 13, 2010.
- Copyright © 2010 by Cold Spring Harbor Laboratory Press