The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100
Copyright policy )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. Biochemical analysis of a fraction enriched in nuclei reveals that nuclear Rmt2 is resistant to extractions with salt and detergent, indicating an association with structural components. This was supported by affinity purification experiments with TAP-tagged Rmt2. Rmt2 was found to co-purify with the nucleoporins Nup49, Nup57 and Nup100, revealing a novel link between arginine methyltransferases and the nuclear pore complex. In addition, a genome-wide transcription study of the rmt2Delta mutant shows significant downregulation of the transcription of MYO1, encoding the Type II myosin heavy chain required for cytokinesis and cell separation.
- Södertörn University Sweden
- King’s University United States
- Children's Hospital Oakland Research Institute United States
- Umeå University Sweden
- University of Chicago United States
Cell Nucleus, Cytoplasm, Protein-Arginine N-Methyltransferases, Saccharomyces cerevisiae Proteins, Myosin Heavy Chains, Nuclear Envelope, Fluorescent Antibody Technique, Methyltransferases, Saccharomyces cerevisiae, Arginine, Methylation, Cell Compartmentation, Nuclear Pore Complex Proteins, Mutation, Protein Processing, Post-Translational, Cytokinesis
Cell Nucleus, Cytoplasm, Protein-Arginine N-Methyltransferases, Saccharomyces cerevisiae Proteins, Myosin Heavy Chains, Nuclear Envelope, Fluorescent Antibody Technique, Methyltransferases, Saccharomyces cerevisiae, Arginine, Methylation, Cell Compartmentation, Nuclear Pore Complex Proteins, Mutation, Protein Processing, Post-Translational, Cytokinesis
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