Ime4 is the catalytic subunit of a conserved methyltransferase (MTase) complex found in yeast, S. cerevisiae. This complex is responsible for creating the RNA modification N6- methyladenosine (m6A), the most common post-transcriptional modification in higher eukaryotes. There is evidence to suggest that m6A is an important mediator of gene expression control within the cell and has been associated with a diverse array of phenotypic effects, notably as a conserved determinant of cell fate. The MTase complex is known to be a nuclear protein, the compartment where it is believed to carry out most of its methylation activity. Recently, the nuclear localization signals (NLS) of the subunits of the human MTase complex were experimentally identified, whereas the NLSs of the yeast MTase complex remain unknown. Here, we have experimentally identified the amino acid sequence 517RKYQEFMKSKTGTSHTGTKKIDKK540, located within the C-terminal region, as a putative bipartite NLS for Ime4
