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

  • Posted in Nat Chem Biol, Publications
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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.

  • Posted in Nat Chem Biol, Publications
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