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Nat Chem Biol. 2014 Nov;10(11):927-9. doi: 10.1038/nchembio.1654. Epub 2014 Sep 21.

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

Author information

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.

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.

PMID:
25242552
DOI:
10.1038/nchembio.1654
[Indexed for MEDLINE]

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