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 journalArticle

20 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)4263-4273
Number of pages11
JournalFEBS Journal
Volume283
Issue number23
DOIs
StatePublished - Dec 1 2016
Externally publishedYes

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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  • Cite this

    Herranz, N., Dave, N., Millanes-Romero, A., Pascual-Reguant, L., Morey, LL., Díaz, V. M., Lórenz-Fonfría, V., Gutierrez-Gallego, R., Jerónimo, C., Iturbide, A., Di Croce, L., García de Herreros, A., & Peiró, S. (2016). Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in histone H3. FEBS Journal, 283(23), 4263-4273. https://doi.org/10.1111/febs.13922