The paper “Structural basis for methylarginine-dependent recognition of Aubergine by Tudor” has been published recently as a cover story in Genes & Development. The research work is carried out by Professor XU Ruiming and Professor GONG Weimin’s groups collaborating with Dr. Ruth Lehmann’s group from NYU, USA. They solved the structure of the 11th Tudor domain (Tud11) of drosophila Tudor, and the complex structures of Tud11 binding with 2 symmetrically-dimethylated arginine (sDMA) modified N-terminal peptides of Aubergine. These structures revealed the binding mode of Tudor with sDMA.

Tudor domain exists widely in various organisms and play important roles in epigenetic, gene expression and small RNA regulation. In germ cell line, the proteins with Tudor domain bind to methylated Piwi proteins and regulate the germ cell differentiation by piRNA pathway. The structural information provides mechanistic insights into sDMA-dependent Piwi-Tudor interaction, and the recognition of sDMA by Tudor domains in general.

The work was supported by grants from the Ministry of Science and Technology (2009CB825501 & 2006CB910903 to R.M.X. and W.G.), the Natural Science Foundation of China (90919029 & 3098801 to R.M.X.), Chinese Academy of Sciences (CAS), and the NIH (GM063716 & HD041900 to R.M.X. and R.L.).