Histone Demethylase LSD1 Is a Folate-Binding Protein

摘要: Methylation of lysine residues in histones has been known to serve a regulatory role gene expression. Although enzymatic removal the methyl groups was discovered as early 1973, enzymes responsible for their were isolated and mechanism action described only recently. The first enzyme show such activity LSD1, flavin-containing that removes from lysines 4 9 histone 3 with generation formaldehyde group. This reaction is similar previously demethylation reactions conducted by dimethylglycine dehydrogenase sarcosine dehydrogenase, which protein-bound tetrahydrofolate serves an accepter generated. We now nuclear extracts HeLa cells contain LSD1 associated folate. Using method back-scattering interferometry, we have measured binding various forms folate both full-length truncated form free solution. 6R,S natural pentaglutamate bound highest affinity (K(d) = 2.8 μM) LSD1. fact participates provides opportunity this micronutrient play epigenetic control