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Updated: Oct 15, 2025

Application of MassSQUIRM for Quantitative Measurements of Lysine Demethylase Activity
Published on: March 11, 2012
Structure, Activity, and Function of the Protein Lysine Methyltransferase G9a
Coralie Poulard1,2,3, Lara M Noureddine1,2,3,4, Ludivine Pruvost1,2,3
1Cancer Research Cancer of Lyon, Université de Lyon, F-69000 Lyon, France.
Abstract:
G9a is a lysine methyltransferase catalyzing the majority of histone H3 mono- and dimethylation at Lys-9 (H3K9), responsible for transcriptional repression events in euchromatin. G9a has been shown to methylate various lysine residues of non-histone proteins and acts as a coactivator for several transcription factors. This review will provide an overview of the structural features of G9a and its paralog called G9a-like protein (GLP), explore the biochemical features of G9a, and describe its post-translational modifications and the specific inhibitors available to target its catalytic activity. Aside from its role on histone substrates, the review will highlight some non-histone targets of G9a, in order gain insight into their role in specific cellular mechanisms. Indeed, G9a was largely described to be involved in embryonic development, hypoxia, and DNA repair. Finally, the involvement of G9a in cancer biology will be presented.
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