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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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PubMed ID:: 20713507

PMC ID:: 2932969

DOI:: 10.1101/gad.1956010

ScienceOpen disciplines: Chemistry

Keywords: Amino Acid Sequence,Animals,Arginine,analogs & derivatives,chemistry,metabolism,Conserved Sequence,Drosophila Proteins,Drosophila melanogaster,genetics,Germ Cells,growth & development,Membrane Transport Proteins,Models, Molecular,Molecular Sequence Data,Peptide Initiation Factors,Protein Binding,Protein Structure, Quaternary,Protein Structure, Tertiary,Sequence Alignment

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ScienceOpen disciplines: Chemistry

Keywords: Amino Acid Sequence, Animals, Arginine, analogs & derivatives, chemistry, metabolism, Conserved Sequence, Drosophila Proteins, Drosophila melanogaster, genetics, Germ Cells, growth & development, Membrane Transport Proteins, Models, Molecular, Molecular Sequence Data, Peptide Initiation Factors, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, Sequence Alignment

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