作者: Federico Forneris , Claudia Binda , MariaAntonietta Vanoni , Andrea Mattevi , Elena Battagliol
DOI: 10.1016/S1874-6047(06)80010-7
关键词: Genetics 、 Histone H3 、 Histone lysine methylation 、 Histone methyltransferase 、 Histone H1 、 Histone octamer 、 Histone methylation 、 Histone code 、 Cell biology 、 Biology 、 Histone H2A
摘要: Histone lysine methylation is one of the posttranslational modifications involved in transcriptional regulation and chromatin remodeling. The first specific histone demethylase (LSD1) has been recently discovered, whichrules out hypothesis that represents a permanent epigenetic mark. LSD1 (previously known as KIAA0601) typically found association with CoREST (a corepressor protein) deacetylases 1 2, forming highly conserved core complex. These proteins have shown to be part several megadalton complexes, which are proposed operate context stable extended form repression through silencing entire domains. FAD-dependent protein specifically catalyzes demethylation Lys4 H3 by an oxidative process. amino acid sequence human enzyme (90 kDa) modular organization N-terminal SWIRM domain, mediate protein-protein interactions, C-terminal domain similar amine oxidases. Three assays based on different events reaction can used study biochemical properties. strict substrate specificity suggests existence other putative demethylases may use alternative mechanisms for this modification.