PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family.
Protein arginine methylation is a common post-translational modification that has been implicated in signal transduction, RNA processing, transcriptional regulation, and DNA repair. A search of the human genome for additional members of the protein arginine N-methyltransferase (PRMT) family of enzymes has identified a gene on chromosome 12 that we have ... termed PRMT8. This novel enzyme is most closely related to PRMT1, although it has a distinctive N-terminal region. The unique N-terminal end harbors a myristoylation motif, and we have shown here that PRMT8 is indeed modified by the attachment of a myristate to the glycine residue after the initiator methionine. The myristoylation of PRMT8 results in its association with the plasma membrane. The second singular property of PRMT8 is its tissue-specific expression pattern; it is largely expressed in the brain. A glutathione S-transferase fusion protein of PRMT8 has type I PRMT activity, catalyzing the formation of omega-NG-monomethylated and asymmetrically omega-NG,NG-dimethylated arginine residues on a recombinant glycine- and arginine-rich substrate. PRMT8 is thus an active arginine methyltransferase that is membrane-associated and tissue-specific, two firsts for this family of enzymes.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Arginine, Blotting, Northern, Brain, Catalysis, Cell Membrane, Dimerization, Gene Expression Regulation, Enzymologic, Glutathione Transferase, Glycine, Green Fluorescent Proteins, HeLa Cells, Humans, Immunoprecipitation, Membrane Proteins, Microscopy, Confocal, Molecular Sequence Data, Plasmids, Protein Binding, Protein-Arginine N-Methyltransferases, RNA, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Tissue Distribution, Transcription, Genetic
Amino Acid Motifs, Amino Acid Sequence, Arginine, Blotting, Northern, Brain, Catalysis, Cell Membrane, Dimerization, Gene Expression Regulation, Enzymologic, Glutathione Transferase, Glycine, Green Fluorescent Proteins, HeLa Cells, Humans, Immunoprecipitation, Membrane Proteins, Microscopy, Confocal, Molecular Sequence Data, Plasmids, Protein Binding, Protein-Arginine N-Methyltransferases, RNA, Recombinant Fusion Proteins, Sequence Homology, Amino Acid, Tissue Distribution, Transcription, Genetic
J. Biol. Chem.
Date: Sep. 23, 2005
PubMed ID: 16051612
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