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

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

Dear Editor, 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 methyltransf...

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Veröffentlicht in:Cell research 2014-12, Vol.24 (12), p.1493-1496
Hauptverfasser: Zhu, Tingting, Roundtree, Ian A, Wang, Ping, Wang, Xiao, Wang, Li, Sun, Chang, Tian, Yuan, Li, Jie, He, Chuan, Xu, Yanhui
Format: Artikel
Sprache:eng
Schlagworte:
631/45/535
Adenosine - analogs & derivatives
Adenosine - metabolism
Amino Acid Sequence
Biomedical and Life Sciences
Cell Biology
Crystallography, X-Ray
Humans
Letter to the Editor
Life Sciences
Models, Molecular
Molecular Sequence Data
mRNA
Protein Binding
Protein Structure, Tertiary
RNA - metabolism
RNA-Binding Proteins - chemistry
RNA-Binding Proteins - metabolism
Sequence Alignment
信使RNA
晶体结构
机制
核糖体RNA
识别
转移RNA
非编码RNA
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Zusammenfassung:Dear Editor, 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 modification [2-6]. This modification plays important roles in various biological processes, including circadian rhythms [7],
ISSN:1001-0602
1748-7838
DOI:10.1038/cr.2014.152