Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in histone H3

Nicolás Herranz, Natàlia Dave, Alba Millanes-Romero, Laura Pascual-Reguant, Lluis Morey, Víctor M. Díaz, Víctor Lórenz-Fonfría, Ricardo Gutierrez-Gallego, Celia Jerónimo, Ane Iturbide, Luciano Di Croce, Antonio García de Herreros, Sandra Peiró

    Research output: Contribution to journalArticleResearchpeer-review

    23 Citations (Scopus)

    Abstract

    © 2016 Federation of European Biochemical Societies 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.
    Original languageEnglish
    Pages (from-to)4263-4273
    JournalFEBS Journal
    Volume283
    Issue number23
    DOIs
    Publication statusPublished - 1 Dec 2016

    Keywords

    • epigenetics
    • histone modification
    • lysyl oxidase-like 2
    • snail1
    • transcriptional regulation

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