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: 1490-1492

LETTERS TO THE EDITOR

Structure of the YTH domain of human YTHDF2 in complex with an m⁶A mononucleotide reveals an aromatic cage for m⁶A recognition

Fudong Li^1,*, Debiao Zhao^1,*, Jihui Wu¹ and Yunyu Shi¹

¹Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Correspondence: Jihui Wu, E-mail: wujihui@ustc.edu.cn; Yunyu Shi,(yyshi@ustc.edu.cn)

Recent discoveries suggest that N6-methyladenosine (m6A) modification, a prevalent internal modification in eukaryotic RNA, is an essential RNA regulatory mechanism. This modification is post-transcriptionally installed by m6A methyltransferases (METTL3-METTL14-WTAP complex)1,2,3,4 and oxidatively removed by m6A demethylases (FTO and ALKBH5)5,6. These 'writer' and 'eraser' enzymes are required for embryo development, energy homeostasis and fertility, suggesting fundamental regulatory roles of m6A1,2,5.

10.1038/cr.2014.153

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