Title:Structural and Functional Characterization of the Proteins Responsible for N6-Methyladenosine Modification and Recognition
Volume: 17
Issue: 4
Author(s): Ke Liu, Yumin Ding, Weiyuan Ye, Yanli Liu, Jihong Yang, Jinlin Liu and Chao Qi
Affiliation:
Keywords:
m6A, RNA methyltransferase and demethylase, YTH domain.
Abstract: RNA modification, involving in a wide variety of cellular processes, has
been identified over 100 types since 1950s. N6-methyladenosine (m6A), as one of the
most abundant RNA modifications, is found in several RNA species and predominantly
located in the stop codons, long internal exons as well as 3’UTR. It was reported
that m6A modification preferentially appears after G in the conserved motif
RRm6ACH (R = A/G and H = A/C/U). There are two families of enzymes responsible
for maintaining the balance of m6A modification: m6A methyltransferases and demethylases, which add and remove
methyl marks for adenosine of RNA, respectively. METTL3 complex, the m6A methyltransferases, and two
kinds of demethylases including Fat mass and obesity-associated protein (FTO) and alkylation protein AlkB homolog
5 (ALKBH5) are characterized thus far. Besides the “writers” and “erasers”, m6A specific recognizing proteins, such
as the YTH (YT521-B homology) domain family proteins, also have attracted significant attention. Herein, we focus
on the recent progress in understanding the biological/biochemical functions and structures of proteins responsible for
the m6A modification and recognition. Detailed analyses of these important proteins are essential for the further study
of their biological function and will also guide us in designing more potent and specific small-molecule chemical inhibitors
for these targets.
