Corrigendum: Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain
September 17th, 2015 by Chao Xu
Nature Chemical Biology 11, 815 (2015). doi:10.1038/nchembio1015-815c
Author: Chao Xu, Xiao Wang, Ke Liu, Ian A Roundtree, Wolfram Tempel, Yanjun Li, Zhike Lu, Chuan He & Jinrong Min
Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain
September 21st, 2014 by Chao Xu
Nature Chemical Biology 10, 927 (2014). doi:10.1038/nchembio.1654
Authors: Chao Xu, Xiao Wang, Ke Liu, Ian A Roundtree, Wolfram Tempel, Yanjun Li, Zhike Lu, Chuan He & Jinrong Min
N6-methyladenosine (m6A) is the most abundant internal modification of nearly all eukaryotic mRNAs and has recently been reported to be recognized by the YTH domain family proteins. Here we present the crystal structures of the YTH domain of YTHDC1, a member of the YTH domain family, and its complex with an m6A-containing RNA. Our structural studies, together with transcriptome-wide identification of YTHDC1-binding sites and biochemical experiments, not only reveal the specific mode of m6A-YTH binding but also explain the preferential recognition of the GG(m6A)C sequences by YTHDC1.