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

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.

SUBMITTER: Liu H

PROVIDER: S-EPMC2932969 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature

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

Liu Haiping H Wang Ju-Yu S JY Huang Ying Y Li Zhizhong Z Gong Weimin W Lehmann Ruth R Xu Rui-Ming RM

Genes & development 20100816 17

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 positi ...[more]

PMID: 20713507

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