Cryo-EM structures of human m⁶A writer complexes.

ABSTRACT: N⁶-methyladenosine (m⁶A) is the most abundant ribonucleotide modification among eukaryotic messenger RNAs. The m⁶A "writer" consists of the catalytic subunit m⁶A-METTL complex (MAC) and the regulatory subunit m⁶A-METTL-associated complex (MACOM), the latter being essential for enzymatic activity. Here, we report the cryo-electron microscopy (cryo-EM) structures of MACOM at a 3.0-Å resolution, uncovering that WTAP and VIRMA form the core structure of MACOM and that ZC3H13 stretches the conformation by binding VIRMA. Furthermore, the 4.4-Å resolution cryo-EM map of the MACOM-MAC complex, combined with crosslinking mass spectrometry and GST pull-down analysis, elucidates a plausible model of the m⁶A writer complex, in which MAC

SUBMITTER: Su S 

PROVIDER: S-EPMC9652331 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature