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Background：
Histone H3 forms H3-H4 tetramers to build nucleosome core scaffold. Its lysine residues undergo diverse reversible post-translational modifications including malonylation and methylation, catalyzed by modifying enzymes and erased by demodifying enzymes. Modifications alter nucleosome compactness and recruit specific reader proteins to regulate transcription, metabolism, DNA repair and cell fate. Different lysine sites carry distinct epigenetic functions. Lysine malonylation is a metabolism-sensitive acyl modification closely linked to glycolysis. H3K23 malonylation (H3K23mal) accumulates at promoters of glycolytic and stress-response genes. It relaxes chromatin structure to boost gene transcription, and its global level directly reflects intracellular malonyl-CoA concentration. Abnormal H3K23mal exists in metabolic disorders and malignant tumors.
