TAILIEUCHUNG - Báo cáo khoa học: New roles of flavoproteins in molecular cell biology: Histone demethylase LSD1 and chromatin

Lysine-specific demethylase 1 (LSD1) is an enzyme that removes methyl groups from mono- and dimethylated Lys4 of histone H3, a post-transla-tional modification associated with gene activation. Human LSD1 was the first histone demethylase to be discovered and this enzymatic activity is conserved among eukaryotes. | MINIREVIEW New roles of flavoproteins in molecular cell biology Histone demethylase LSD1 and chromatin Federico Forneris1 Elena Battaglioli2 Andrea Mattevi1 and Claudia Binda1 1 Dipartimento di Genetica e Microbiologia Universita di Pavia Italy 2 Dipartimento di Biologia e Genetica per le Scienze Mediche University di Milano Italy Keywords amine oxidase domain chromatin epigenetics enzyme flavin gene expression histone demethylation hydrogen peroxide protein complex Rossmann fold Correspondence C. Binda Dipartimento di Genetica e Microbiologia Universita di Pavia Via Ferrata 1 27100 Pavia Italy Fax 39 382 528496 Tel 39 382 985534 E-mail binda@ Website http biocry Received 6 January 2009 revised 21 May 2009 accepted 22 May 2009 doi Lysine-specific demethylase 1 LSD1 is an enzyme that removes methyl groups from mono- and dimethylated Lys4 of histone H3 a post-translational modification associated with gene activation. Human LSD1 was the first histone demethylase to be discovered and this enzymatic activity is conserved among eukaryotes. LSD1 has been identified in a number of chromatin-remodeling complexes that control gene transcription and its demethylase activity has also been linked to pathological processes including tumorigenesis. The 852-residue sequence of LSD1 comprises an amine oxidase domain which identifies a family of enzymes that catalyze the FAD-dependent oxidation of amine substrates ranging from amino acids to aromatic neurotransmitters. Among these proteins LSD1 is peculiar in that it acts on a protein substrate in the nuclear environment of chromatinremodeling complexes. This functional divergence occurred during evolution from the eubacteria to eukaryotes by acquisition of additional domains such as the SWIRM domain. The N-terminal part of LSD1 predicted to be disordered contains linear motifs that might represent functional sites responsible for the association of this enzyme with a .

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