Tags

Type your tag names separated by a space and hit enter

PRMT-5 converts monomethylarginines into symmetrical dimethylarginines in Caenorhabditis elegans.
J Biochem. 2017 02 01; 161(2):231-235.JB

Abstract

The transmethylation to arginine residues of proteins is catalyzed by protein arginine methyltransferases (PRMTs) that form monomethylarginine (MMA), asymmetric (ADMA) and symmetric dimethylarginines (SDMA). Although we previously demonstrated that the generation of ADMA residues in whole proteins is driven by PRMT-1 in Caenorhabditis elegans, much less is known about MMA and SDMA in vivo. In this study, we measured the amounts of different methylarginines in whole protein extracts made from wild-type (N2) C. elegans and from prmt-1 and prmt-5 null mutants using liquid chromatography-tandem mass spectrometry. Interestingly, we found that the amounts of MMA and SDMA are about fourfold higher than those of ADMA in N2 protein lysates using acid hydrolysis. We were unable to detect SDMA residues in the prmt-5 null mutant. In comparison with N2, an increase in SDMA and decrease in MMA were observed in prmt-1 mutant worms with no ADMA, but ADMA and MMA levels were unchanged in prmt-5 mutant worms. These results suggest that PRMT-1 contributes, at least in part, to MMA production, but that PRMT-5 catalyzes the symmetric dimethylation of substrates containing MMA residues in vivo.

Links

Publisher Full Text (DOI)

Authors+Show Affiliations

Kanou A
Graduate School of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8577, Japan.
Kako K
Faculty of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8577, Japan.
Hirota K
Faculty of Life and Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8577, Japan. PhD Program in Human Biology, School of Integrative and Global Majors, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8577, Japan.
Fukamizu A
Life Science Center of Tsukuba Advanced Research Alliance, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8577, Japan.

MeSH

AnimalsArginineCaenorhabditis elegansCaenorhabditis elegans ProteinsChromatography, LiquidMethylationMutationProtein-Arginine N-MethyltransferasesTandem Mass Spectrometry

Pub Type(s)

Journal Article

Language

eng

PubMed ID

28173048

Citation

Kanou, Akihiko, et al. "PRMT-5 Converts Monomethylarginines Into Symmetrical Dimethylarginines in Caenorhabditis Elegans." Journal of Biochemistry, vol. 161, no. 2, 2017, pp. 231-235.
Kanou A, Kako K, Hirota K, et al. PRMT-5 converts monomethylarginines into symmetrical dimethylarginines in Caenorhabditis elegans. J Biochem. 2017;161(2):231-235.
Kanou, A., Kako, K., Hirota, K., & Fukamizu, A. (2017). PRMT-5 converts monomethylarginines into symmetrical dimethylarginines in Caenorhabditis elegans. Journal of Biochemistry, 161(2), 231-235. https://doi.org/10.1093/jb/mvw066
Kanou A, et al. PRMT-5 Converts Monomethylarginines Into Symmetrical Dimethylarginines in Caenorhabditis Elegans. J Biochem. 2017 02 1;161(2):231-235. PubMed PMID: 28173048.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - PRMT-5 converts monomethylarginines into symmetrical dimethylarginines in Caenorhabditis elegans. AU - Kanou,Akihiko, AU - Kako,Koichiro, AU - Hirota,Keiko, AU - Fukamizu,Akiyoshi, PY - 2016/09/13/received PY - 2016/10/13/accepted PY - 2017/2/8/entrez PY - 2017/2/9/pubmed PY - 2017/5/4/medline KW - Caenorhabditis elegans KW - arginine methylation KW - protein arginine methyltransferase KW - acid hydrolysis KW - LC-MS/MS SP - 231 EP - 235 JF - Journal of biochemistry JO - J Biochem VL - 161 IS - 2 N2 - The transmethylation to arginine residues of proteins is catalyzed by protein arginine methyltransferases (PRMTs) that form monomethylarginine (MMA), asymmetric (ADMA) and symmetric dimethylarginines (SDMA). Although we previously demonstrated that the generation of ADMA residues in whole proteins is driven by PRMT-1 in Caenorhabditis elegans, much less is known about MMA and SDMA in vivo. In this study, we measured the amounts of different methylarginines in whole protein extracts made from wild-type (N2) C. elegans and from prmt-1 and prmt-5 null mutants using liquid chromatography-tandem mass spectrometry. Interestingly, we found that the amounts of MMA and SDMA are about fourfold higher than those of ADMA in N2 protein lysates using acid hydrolysis. We were unable to detect SDMA residues in the prmt-5 null mutant. In comparison with N2, an increase in SDMA and decrease in MMA were observed in prmt-1 mutant worms with no ADMA, but ADMA and MMA levels were unchanged in prmt-5 mutant worms. These results suggest that PRMT-1 contributes, at least in part, to MMA production, but that PRMT-5 catalyzes the symmetric dimethylation of substrates containing MMA residues in vivo. SN - 1756-2651 UR - https://www.unboundmedicine.com/medline/citation/28173048/PRMT_5_converts_monomethylarginines_into_symmetrical_dimethylarginines_in_Caenorhabditis_elegans_ DB - PRIME DP - Unbound Medicine ER -