PRMT-5 converts monomethylarginines into symmetrical dimethylarginines in Caenorhabditis elegans.

doi:10.1093/jb/mvw066

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Article

PRMT-5 converts monomethylarginines into symmetrical dimethylarginines in Caenorhabditis elegans.

Journal of biochemistry - 1 Feb 2017

Kanou Akihiko, Kako Koichiro, Hirota Keiko, Fukamizu Akiyoshi

Abstract excerpt

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...

Topics

Animals
Arginine
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Chromatography, Liquid
Methylation
Mutation
Protein-Arginine N-Methyltransferases
Tandem Mass Spectrometry

Source

Open in PubMed

Identifiers

PMID: 28173048
DOI: 10.1093/jb/mvw066

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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