Volume 24, No 12, Dec 2014

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 24 Issue 12, December 2014: 1493-1496

LETTERS TO THE EDITOR

Crystal structure of the YTH domain of YTHDF2 reveals mechanism for recognition of N6-methyladenosine

Tingting Zhu¹, Ian A Roundtree², Ping Wang1, Xiao Wang^3,4, Li Wang¹, Chang Sun¹, Yuan Tian¹, Jie Li¹, Chuan He^3,4 and Yanhui Xu¹

¹Fudan University Shanghai Cancer Center, Department of Oncology; and Institute of Biomedical Sciences and School of Basic Medical Sciences, Shanghai Medical College of Fudan University, Shanghai 200032, China
²Medical Scientist Training Program and Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA
³Department of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637, USA
⁴Howard Hughes Medical Institute, The University of Chicago, Chicago, IL 60637, USA Correspondence: Yanhui Xu,(xuyh@fudan.edu.cn)

N6-methyladenosine (m6A) has been demonstrated to be ubiquitous in several types of eukaryotic RNAs, including messenger RNA (mRNA), transfer RNA (tRNA), ribosomal RNA (rRNA), long non-coding RNA (lncRNA), and small nuclear RNA (snRNA)1. The recent discoveries of RNA m6A methyltransferase complex METTL3/METTL14/WTAP and demethylases FTO and ALKBH5 prove the reversibility of m6A modification2,3,4,5,6. This modification plays important roles in various biological processes, including circadian rhythms7, RNA splicing8,

10.1038/cr.2014.152

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