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Updated: Jun 5, 2025

Exploring the Arginine Methylome by Nuclear Magnetic Resonance Spectroscopy
Published on: December 16, 2021
Lysine and arginine methylation of transcription factors
Benedetto Daniele Giaimo1, Francesca Ferrante2, Tilman Borggrefe3
1Institute of Biochemistry, Justus-Liebig-University Giessen, Friedrichstrasse 24, 35392, Giessen, Germany. Benedetto.Giaimo@biochemie.med.uni-giessen.de.
Abstract:
Post-translational modifications (PTMs) are implicated in many biological processes including receptor activation, signal transduction, transcriptional regulation and protein turnover. Lysine's side chain is particularly notable, as it can undergo methylation, acetylation, SUMOylation and ubiquitination. Methylation affects not only lysine but also arginine residues, both of which are implicated in epigenetic regulation. Beyond histone-tails as substrates, dynamic methylation of transcription factors has been described. The focus of this review is on these non-histone substrates providing a detailed discussion of what is currently known about methylation of hypoxia-inducible factor (HIF), P53, nuclear receptors (NRs) and RELA. The role of methylation in regulating protein stability and function by acting as docking sites for methyl-reader proteins and via their crosstalk with other PTMs is explored.
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