Journal
GENES & DEVELOPMENT
Volume 24, Issue 17, Pages 1876-1881Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1956010
Keywords
Tudor; Aubergine; Piwi; arginine methylation; structure
Categories
Funding
- Ministry of Science and Technology [2009CB825501, 2006CB910903]
- Natural Science Foundation of China [90919029, 3098801]
- Chinese Academy of Sciences (CAS)
- NIH [GM063716]
Ask authors/readers for more resources
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 thats DMA 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available