Three years after its discovery, lysine-specific demethylase 1 remains at the forefront of chromatin research. Its demethylase activity on Lys4 of histone H3 supports its role in gene repression. By contrast, the biochemical mechanisms underlying lysine-specific demethylase 1 involvement in transcriptional activation are not firmly established. Structural studies highlight a specific binding site for the histone H3 N-terminal tail and a catalytic machinery that is closely related to that of other flavin-dependent amine oxidases. These insights are crucial for the development of demethylation inhibitors. Furthermore, the exploration of putative non-histone substrates and potential signaling roles of hydrogen peroxide produced by the demethylation reaction could lead to new paradigms in chromatin biology.
|Titolo:||LSD1 : oxidative chemistry for multifaceted functions in chromatin regulation|
|Autori interni:||BATTAGLIOLI, ELENA (Penultimo)|
|Settore Scientifico Disciplinare:||Settore BIO/13 - Biologia Applicata|
|Data di pubblicazione:||apr-2008|
|Digital Object Identifier (DOI):||10.1016/j.tibs.2008.01.003|
|Appare nelle tipologie:||01 - Articolo su periodico|