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

被引：23

作者：

Xu, Chao ^{[1
]}

Wang, Xiao ^{[2
,3
,4
]}

Liu, Ke ^{[1
]}

Roundtree, Ian A. ^{[4
,5
,6
]}

Tempel, Wolfram ^{[1
]}

Li, Yanjun ^{[1
,3
]}

Lu, Zhike ^{[2
,3
,4
]}

He, Chuan ^{[2
,4
]}

Min, Jinrong ^{[1
,7
]}

机构：

[1] Univ Toronto, Struct Genom Consortium, Toronto, ON, Canada

[2] Univ Chicago, Dept Chem, Chicago, IL 60637 USA

[3] Univ Chicago, Inst Biophys Dynam, Chicago, IL 60637 USA

[4] Univ Chicago, Howard Hughes Med Inst, Chicago, IL 60637 USA

[5] Univ Chicago, Med Scientist Training Program, Chicago, IL 60637 USA

[6] Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA

[7] Univ Toronto, Dept Physiol, Toronto, ON, Canada

来源：

NATURE CHEMICAL BIOLOGY | 2014年 / 10卷 / 11期

基金：

英国惠康基金; 加拿大创新基金会; 美国国家科学基金会;

关键词：

NUCLEAR-RNA; PROTEIN; N6-METHYLADENOSINE; REVEALS; SITES;

D O I：

10.1038/NCHEMBIO.1654

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：927 / 929

页数：3

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