YTH Domain: A Family of N-methyladenosine (mA) Readers.
10.1016/j.gpb.2018.04.002
- Author:
Shanhui LIAO
1
;
Hongbin SUN
2
;
Chao XU
3
,
4
Author Information
1. Heifei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, China.
2. School of Food and Biological Engineering, Zhengzhou University of Light Industry, Zhengzhou 450002, China. Electronic address: hbsun@mail.ustc.edu.cn.
3. Heifei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei 230027, China
4. CAS Key Laboratory of Structural Biology, University of Science and Technology of China, Hefei 230027, China. Electronic address: xuchaor@ustc.edu.cn.
- Publication Type:Journal Article
- Keywords:
Epitranscriptome;
RNA demethylation;
RNA methylation;
RNA modification;
YT521-B homology
- MeSH:
Adenosine;
analogs & derivatives;
chemistry;
metabolism;
Animals;
Humans;
Protein Binding;
Protein Domains;
RNA;
chemistry;
metabolism;
RNA-Binding Proteins;
chemistry;
metabolism
- From:
Genomics, Proteomics & Bioinformatics
2018;16(2):99-107
- CountryChina
- Language:English
-
Abstract:
Like protein and DNA, different types of RNA molecules undergo various modifications. Accumulating evidence suggests that these RNA modifications serve as sophisticated codes to mediate RNA behaviors and many important biological functions. N-methyladenosine (mA) is the most abundant internal RNA modification found in a variety of eukaryotic RNAs, including but not limited to mRNAs, tRNAs, rRNAs, and long non-coding RNAs (lncRNAs). In mammalian cells, mA can be incorporated by a methyltransferase complex and removed by demethylases, which ensures that the mA modification is reversible and dynamic. Moreover, mA is recognized by the YT521-B homology (YTH) domain-containing proteins, which subsequently direct different complexes to regulate RNA signaling pathways, such as RNA metabolism, RNA splicing, RNA folding, and protein translation. Herein, we summarize the recent progresses made in understanding the molecular mechanisms underlying the mA recognition by YTH domain-containing proteins, which would shed new light on mA-specific recognition and provide clues to the future identification of reader proteins of many other RNA modifications.
