Characterization of MYR1, a dosage suppressor of YPT6 and RIC1 deficient mutants.

Membrane traffic is tightly regulated and the Rab protein family of small GTPases plays a central role in this regulation. One member of this family is the Saccharomyces cerevisae protein Ypt6. To search for new genes interacting with Ypt6-related pathways, we performed a genetic screen for high copy suppressors of ypt6Delta temperature sensitivity at 35 degrees C.

The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100.

Arginine methylation is a post-translational modification of proteins implicated in RNA processing, protein compartmentalization, signal transduction, transcriptional regulation and DNA repair. In a screen for proteins associated with the nuclear envelope in the yeast Saccharomyces cerevisiae, we have identified the arginine methyltransferase Rmt2, previously shown to methylate the ribosomal protein L12. By indirect immunofluorescence and subcellular fractionations we demonstrate here that Rmt2 has nuclear and cytoplasmic localizations.