N⁶-methyladenosine (m⁶A) is the most abundant mRNA modification in eukaryotes, playing crucial roles in multiple biological processes. m⁶A is catalyzed by the activity of methyltransferase-like 3 (Mettl3), which depends on additional proteins whose precise functions remain poorly understood. Here we identified Zc3h13 (zinc finger CCCH domain-containing protein 13)/Flacc [Fl(2)d-associated complex component] as a novel interactor of m⁶A methyltransferase complex components in Drosophila and mice. Like other components of this complex, Flacc controls m⁶A levels and is involved in sex determination in Drosophila We demonstrate that Flacc promotes m⁶A deposition by bridging Fl(2)d to the mRNA-binding factor Nito. Altogether, our work advances the molecular understanding of conservation and regulation of the m⁶A machinery.
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Knuckles et al. (2018) studied this question.
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