The yeast RNA methylation complex consists of conserved yet reconfigured components with m6A-dependent and independent roles [RNA-Seq]
N6-methyladenosine (m6A), the most abundant mRNA modification, is  deposited in mammals/drosophila/plants by m6A methyltransferase complexes (MTC) comprising a catalytic subunit and at least five additional proteins. The yeast  MTC is critical for meiosis but was known to comprise three proteins, of which  two were conserved. We uncover three novel MTC components (Kar4/Ygl036w-Vir1/Dyn2). All MTC subunits, except for Dyn2, are essential for m6A deposition and have corresponding mammalian MTC orthologs. Unlike the mammalian bipartite MTC, the yeast MTC is unipartite, yet multifunctional. The MTC's mRNA interacting core, comprising Ime4, Mum2, Vir1, and Kar4, is critical for the m6A-independent function in meiosis, while the MTC's catalytic activity is enabled by Slz1 during meiosis. Kar4 also has a mechanistically separate function from the MTC during mating. Our findings demonstrate that the yeast MTC constituents play distinguishable m6A-dependent, MTC-dependent and-independent functions, highlighting its complexity and paving the path to dissecting the multi-layered functions in mammals. Overall design: poly-A- enriched RNA from SK1 S.cerevisiae during synchronized sporulation induction, for different deletion strains.