Structural Insights into N-methyladenosine (mA) Modification in the Transcriptome.
10.1016/j.gpb.2018.03.001
- Author:
Jinbo HUANG
1
;
Ping YIN
2
Author Information
1. National Key Laboratory of Crop Genetic Improvement and National Center of Plant Gene Research, Huazhong Agricultural University, Wuhan 430070, China.
2. National Key Laboratory of Crop Genetic Improvement and National Center of Plant Gene Research, Huazhong Agricultural University, Wuhan 430070, China. Electronic address: yinping@mail.hzau.edu.cn.
- Publication Type:Journal Article
- Keywords:
Epitranscriptomics;
Eraser;
M(6)A modification;
Reader;
Writer
- MeSH:
Adenosine;
analogs & derivatives;
metabolism;
Animals;
Gene Expression Regulation;
Humans;
Methyltransferases;
chemistry;
metabolism;
RNA, Messenger;
chemistry;
metabolism;
RNA, Untranslated;
chemistry;
metabolism;
RNA-Binding Proteins;
chemistry;
metabolism;
Transcriptome
- From:
Genomics, Proteomics & Bioinformatics
2018;16(2):85-98
- CountryChina
- Language:English
-
Abstract:
More than 100 types of chemical modifications in RNA have been well documented. Recently, several modifications, such as N-methyladenosine (mA), have been detected in mRNA, opening the window into the realm of epitranscriptomics. The mA modification is the most abundant modification in mRNA and non-coding RNA (ncRNA). At the molecular level, mA affects almost all aspects of mRNA metabolism, including splicing, translation, and stability, as well as microRNA (miRNA) maturation, playing essential roles in a range of cellular processes. The mA modification is regulated by three classes of proteins generally referred to as the "writer" (adenosine methyltransferase), "eraser" (mA demethylating enzyme), and "reader" (mA-binding protein). The mA modification is reversibly installed and removed by writers and erasers, respectively. Readers, which are members of the YT521-B homology (YTH) family proteins, selectively bind to RNA and affect its fate in an mA-dependent manner. In this review, we summarize the structures of the functional proteins that modulate the mA modification, and provide our insights into the mA-mediated gene regulation.
