Structure and domain organization of Drosophila Tudor
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Dear Editor,Drosophila tudor is a maternal effect gene required for germ cell formation and abdominal segmentation during oogenesis ”1,2”.It encodes a large protein,Tudor (Tud),of 2 515 amino acids,containing 11 copies of a ~60-residue sequence motif,termed the tudor domain.Tudor domains are best characterized by their methyllysine and methylarginine binding abilities ”3-5”.Biochemically,Tud interacts with Aubergine (Aub),a Piwi family protein,in a manner dependent on symmetrically dimethylated arginine (sDMA) residues located at the N-terminal end of Aub ”6-8”.The sDMA-dependent interaction between Tud and Aub is part of a broad range of phenomena involving tudor domain and Piwi family proteins,in species ranging from fruit flies to mammals ”3”.
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The work is supported by the ”Key New Drug Creation and Manufacturing Program” of China 2014ZX09507-002,and grants from the National Natural Science Foundation of China 31370734,91219307 and 31210103914,and the Strategic Priority Research Program XDB08010100 and the Key Research Program KJZD-EW-L05 of Chinese Academy of Sciences.