2. Academic Validation
  3. Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain

Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain

  • Nat Chem Biol. 2014 Nov;10(11):927-9. doi: 10.1038/nchembio.1654.
Chao Xu 1,  Xiao Wang 2,  Ke Liu 3,  Ian A Roundtree 4,  Wolfram Tempel 5,  Yanjun Li 5,  Zhike Lu 6,  Chuan He 6,  Jinrong Min 7
Affiliations

Affiliations

  • 1 1] Structural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada. [2]. chaor.xu@utoronto.edu.
  • 2 1] Department of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois, USA. [2] Howard Hughes Medical Institute, The University of Chicago, Chicago, Illinois, USA. [3].
  • 3 1] Structural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada. [2].
  • 4 1] Howard Hughes Medical Institute, The University of Chicago, Chicago, Illinois, USA. [2] Medical Scientist Training Program and Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.
  • 5 Structural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada.
  • 6 1] Department of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois, USA. [2] Howard Hughes Medical Institute, The University of Chicago, Chicago, Illinois, USA.
  • 7 1] Structural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada. [2] Department of Physiology, University of Toronto, Toronto, Ontario, Canada.
PMID: 25242552 DOI: 10.1038/nchembio.1654
Abstract

N(6)-methyladenosine (m(6)A) 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 m(6)A-containing RNA. Our structural studies, together with transcriptome-wide identification of YTHDC1-binding sites and biochemical experiments, not only reveal the specific mode of m(6)A-YTH binding but also explain the preferential recognition of the GG(m(6)A)C sequences by YTHDC1.

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