Details

Autor(en) / Beteiligte

• Ren, Ren
• Liu, Haiping
• Wang, Wenjia
• Wang, Mingzhu
• Yang, Na
• Dong, Yu-hui
• Gong, Weimin
• Lehmann, Ruth
• Xu, Rui-Ming

Titel

Structure and domain organization of Drosophila Tudor

Ist Teil von

• Cell research, 2014-09, Vol.24 (9), p.1146-1149

Ort / Verlag

England: Nature Publishing Group

Erscheinungsjahr

2014

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• 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]. We and others have shown previously that domains 7-11 of Tud （Tud7-11） were necessary and sufficient for germ cell formation and interaction with arginine-meth- ylated Aub [9-11]. The structure of Tudl 1 in complex with sDMA-Aub peptides, together with the structure of human SND 1 （TDRD11） bound to sDMA peptides from PIWIL1, uncovered the composition of the sDMA- binding pocket, which consists of a cage of four aromatic residues and an asparagine [10, 12].