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Genes Dev. 2010 Sep 1;24(17):1876-81. doi: 10.1101/gad.1956010. Epub 2010 Aug 16.

Structural basis for methylarginine-dependent recognition of Aubergine by Tudor.

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1
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.

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.

PMID:
20713507
PMCID:
PMC2932969
DOI:
10.1101/gad.1956010
[Indexed for MEDLINE]
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