Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain
Structural basis for selective binding of m6A RNA by the YTHDC1 YTH domain
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DOI：
10.1038/nchembio.1654
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发表时间：
2014-11-01
影响因子：
14.8
通讯作者：
Min, Jinrong
中科院分区：
文献类型：
--
作者：
Xu, Chao;Wang, Xiao;Min, Jinrong
N-6-甲基腺苷（m（6）A）是几乎所有真核生物mRNA中最丰富的内部修饰，最近报道被YTH结构域家族蛋白识别。在这里，我们提出的YTH域的YTHDC 1，YTH域家族的成员，和它的复合物与m（6）A-含有RNA的晶体结构。我们的结构研究，连同转录组范围内YTHDC 1结合位点的鉴定和生化实验，不仅揭示了m（6）A-YTH结合的特异性模式，而且还解释了YTHDC 1优先识别GG（m（6）A）C序列。
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.