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The C. elegans PRMT-3 possesses a type III protein arginine methyltransferase activity.
J Recept Signal Transduct Res. 2011 Apr; 31(2):168-72.JR

Abstract

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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Authors+Show Affiliations

Takahashi Y
The Life Science Center, Tsukuba Advanced Research Alliance, Graduate School of Life and Environmental Sciences,University of Tsukuba, Tsukuba, Ibaraki, Japan.
Daitoku H
No affiliation info available
Yokoyama A
No affiliation info available
Nakayama K
No affiliation info available
Kim JD
No affiliation info available
Fukamizu A
No affiliation info available

MeSH

AnimalsBiocatalysisCaenorhabditis elegansCaenorhabditis elegans ProteinsHistonesHumansMethylationMethyltransferasesPhylogenyProtein BindingProtein-Arginine N-MethyltransferasesS-AdenosylmethionineSequence Homology, Amino Acidomega-N-Methylarginine

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

21385054

Citation

Takahashi, Yuta, et al. "The C. Elegans PRMT-3 Possesses a Type III Protein Arginine Methyltransferase Activity." Journal of Receptor and Signal Transduction Research, vol. 31, no. 2, 2011, pp. 168-72.
Takahashi Y, Daitoku H, Yokoyama A, et al. The C. elegans PRMT-3 possesses a type III protein arginine methyltransferase activity. J Recept Signal Transduct Res. 2011;31(2):168-72.
Takahashi, Y., Daitoku, H., Yokoyama, A., Nakayama, K., Kim, J. D., & Fukamizu, A. (2011). The C. elegans PRMT-3 possesses a type III protein arginine methyltransferase activity. Journal of Receptor and Signal Transduction Research, 31(2), 168-72. https://doi.org/10.3109/10799893.2011.555768
Takahashi Y, et al. The C. Elegans PRMT-3 Possesses a Type III Protein Arginine Methyltransferase Activity. J Recept Signal Transduct Res. 2011;31(2):168-72. PubMed PMID: 21385054.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The C. elegans PRMT-3 possesses a type III protein arginine methyltransferase activity. AU - Takahashi,Yuta, AU - Daitoku,Hiroaki, AU - Yokoyama,Atsuko, AU - Nakayama,Kimihiro, AU - Kim,Jun-Dal, AU - Fukamizu,Akiyoshi, PY - 2011/3/10/entrez PY - 2011/3/10/pubmed PY - 2011/6/17/medline SP - 168 EP - 72 JF - Journal of receptor and signal transduction research JO - J Recept Signal Transduct Res VL - 31 IS - 2 N2 - 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. SN - 1532-4281 UR - https://www.unboundmedicine.com/medline/citation/21385054/The_C__elegans_PRMT_3_possesses_a_type_III_protein_arginine_methyltransferase_activity_ L2 - https://www.tandfonline.com/doi/full/10.3109/10799893.2011.555768 DB - PRIME DP - Unbound Medicine ER -