A new histone oxidation discovered: KDM3A turns acetyl-lysine into hydroxyacetyl-lysine on H3K9
Histone modifications are central to the regulation of eukaryotic transcription, and for decades, the known repertoire of Nε-lysine marks has been limited to acetylation, methylation, and their derivatives. Now, researchers have identified a previously unknown post-translational modification: the oxidation of acetyl-lysine to hydroxyacetyl-lysine on histone H3 lysine 9 (H3K9). This reaction is catalysed by the human JmjC domain-containing demethylase KDM3A, a protein already implicated in the cellular hypoxic response. The finding redefines the functional scope of KDM3A, suggesting that demethylases may also act as oxidases, converting an acetyl group into a new chemical signature with potentially profound implications for epigenetic signaling.
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