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Protein arginine methylation: A prominent modification and its demethylation.
Cell. Mol. Life Sci. 74, 1432-1443 (2017)
Arginine methylation of histones is one mechanism of epigenetic regulation in eukaryotic cells. Methylarginines can also be found in non-histone proteins involved in various different processes in a cell. An enzyme family of nine protein arginine methyltransferases catalyses the addition of methyl groups on arginines of histone and non-histone proteins, resulting in either mono- or dimethylated-arginine residues. The reversibility of histone modifications is an essential feature of epigenetic regulation to respond to changes in environmental factors, signalling events, or metabolic alterations. Prominent histone modifications like lysine acetylation and lysine methylation are reversible. Enzyme family pairs have been identified, with each pair of lysine acetyltransferases/deacetylases and lysine methyltransferases/demethylases operating complementarily to generate or erase lysine modifications. Several analyses also indicate a reversible nature of arginine methylation, but the enzymes facilitating direct removal of methyl moieties from arginine residues in proteins have been discussed controversially. Differing reports have been seen for initially characterized putative candidates, like peptidyl arginine deiminase 4 or Jumonji-domain containing protein 6. Here, we review the most recent cellular, biochemical, and mass spectrometry work on arginine methylation and its reversible nature with a special focus on putative arginine demethylases, including the enzyme superfamily of Fe(II) and 2-oxoglutarate-dependent oxygenases.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Histone Modifications ; Kdm ; Kdm2a ; Kdm3a ; Kdm4e ; Kdm5c ; Kdm6b ; Kdm7b ; Kmt ; Liquid Chromatography–tandem Mass Spectrometry ; Phf8 ; Post-translational Modifications; Proteomic Analysis; Saccharomyces-cerevisiae; Mass-spectrometry; Yeast Proteins; Posttranslational Modifications; Peptidylarginine Deiminases; Lysyl-hydroxylation; Lung Adenocarcinoma; Nonhistone Proteins; Human-cells
ISSN (print) / ISBN
1420-682X
e-ISSN
1420-9071
Quellenangaben
Volume: 74,
Issue: 18,
Pages: 1432-1443
Publisher
Birkhäuser
Publishing Place
Basel
Non-patent literature
Publications
Reviewing status
Peer reviewed