| Literature DB >> 27735137 |
Nicolás Herranz1, Natàlia Dave1, Alba Millanes-Romero1, Laura Pascual-Reguant1, Lluis Morey2, Víctor M Díaz1,3, Víctor Lórenz-Fonfría4, Ricardo Gutierrez-Gallego3, Celia Jerónimo2, Ane Iturbide1, Luciano Di Croce2,3,5, Antonio García de Herreros1,3, Sandra Peiró1.
Abstract
Methylation of histone H3 lysine 4 is linked to active transcription and can be removed by LSD1 or the JmjC domain-containing proteins by amino-oxidation or hydroxylation, respectively. Here we describe that its deamination can be catalyzed by lysyl oxidase-like 2 protein (LOXL2), presenting an unconventional chemical mechanism for H3K4 modification. Infrared spectroscopy and mass spectrometry analyses demonstrated that recombinant LOXL2 specifically deaminates trimethylated H3K4. Moreover, by regulating H3K4me3 deamination, LOXL2 activity is linked with the transcriptional control of the CDH1 gene. These results reveal the existence of further H3 modification as well as a novel mechanism for H3K4me3 demethylation. DATABASE: The GEO accession number for the data referred to this paper is GSE35600.Entities:
Keywords: epigenetics; histone modification; lysyl oxidase-like 2; snail1; transcriptional regulation
Mesh：
Substances：
Year: 2016 PMID： 27735137 DOI： 10.1111/febs.13922
Source DB: PubMed Journal: FEBS J ISSN： 1742-464X Impact factor: 5.542