YTH Domain: A Family of N-methyladenosine (mA) Readers / 基因组蛋白质组与生物信息学报·英文版
Genomics, Proteomics & Bioinformatics
;
(4): 99-107, 2018.
Article
Dans Anglais
| WPRIM
| ID: wpr-772998
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.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Liaison aux protéines
/
ARN
/
Adénosine
/
Chimie
/
Protéines de liaison à l'ARN
/
Domaines protéiques
/
Métabolisme
Limites du sujet:
Animaux
/
Humains
langue:
Anglais
Texte intégral:
Genomics, Proteomics & Bioinformatics
Année:
2018
Type:
Article
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