Journal
JOURNAL OF RECEPTORS AND SIGNAL TRANSDUCTION
Volume 31, Issue 2, Pages 168-172Publisher
TAYLOR & FRANCIS LTD
DOI: 10.3109/10799893.2011.555768
Keywords
Arginine methylation; monomethyl arginine; mammalian PRMT7
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Funding
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [17054004, 20780237, 22688029]
- Grants-in-Aid for Scientific Research [17054004, 22688029, 20780237] Funding Source: KAKEN
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Protein arginine methylation is a common post-translational modification in eukaryotes that is catalyzed by a family of the protein arginine methyltransferases (PRMTs). PRMTs are classified into three types: type I and type II add asymmetrically and symmetrically dimethyl groups to arginine, respectively, while type III adds solely monomethyl group to arginine. However, although the enzymatic activity of type I and type II PRMTs have been reported, the substrate specificity and the methylation activity of type III PRMTs still remains unknown. Here, we report the characterization of Caenorhabditis elegans PRMT-2 and PRMT-3, both of which are highly homologous to human PRMT7. We find that these two PRMTs can bind to S-adenosyl methionine (SAM), but only PRMT-3 has methyltransferase activity for histone H2A depending on its SAM-binding domain. Importantly, thin-layer chromatographic analysis demonstrates that PRMT-3 catalyzes the formation of monomethylated, but not dimethylated arginine. Our study thus identifies the first type III PRMT in C. elegans and provides a means to elucidate the physiological significance of arginine monomethylation in multicellular organisms.
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