Identification of YTH Domain-Containing Proteins as the Readers for N1-Methyladenosine in RNA

被引：191
作者：
Dai, Xiaoxia [1 ]
Wang, Tianlu [1 ]
Gonzalez, Gwendolyn [2 ]
Wang, Yinsheng [1 ,2 ]
机构：
[1] Univ Calif Riverside, Dept Chem, Riverside, CA 92521 USA
[2] Univ Calif Riverside, Environm Toxicol Grad Program, Riverside, CA 92521 USA
来源：
ANALYTICAL CHEMISTRY | 2018年 / 90卷 / 11期
基金：
美国国家卫生研究院;
关键词：
DYNAMIC N-1-METHYLADENOSINE METHYLOME; MESSENGER-RNA; MAPPING REVEALS; TRANSLATION; METHYLATION; N6-METHYLADENOSINE; RECOGNITION; RESOLUTION; PROGRAM; COMPLEX;
D O I：
10.1021/acs.analchem.8b01703
中图分类号：
O65 [分析化学];
学科分类号：
070302 ; 081704 ;
摘要：
Nl-methyladenosine (m(1)A) is an important post-transcriptional modification in RNA; however, the exact biological role of m(1)A remains to be determined. By employing a quantitative proteomics method, we identified multiple putative protein readers of m(1)A in RNA, including several YTH domain family proteins. We showed that YTHDF1-3 and YTHDC1, but not YTHDC2, could bind directly to m(1)A in RNA. We also found that Trp(432) in YTHDF2, a conserved residue in the hydrophobic pocket of the YTH domain that is necessary for its binding to N-6-methyladenosine (m(6)A), is required for its recognition of m(1)A. An analysis of previously published data revealed transcriptome-wide colocalization of YTH domain-containing proteins and m(1)A sites in HeLa cells, suggesting that YTH domain-containing proteins can bind to m(1)A in cells. Together, our results uncovered YTH domain-containing proteins as readers for m(1)A in RNA and provided new insight into the functions of m(1)A in RNA biology.
引用
收藏
页码：6380 / 6384
页数：5
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