Lysyl Oxidase-like 2 Deaminates Lysine 4 in Histone H3

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

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    58 Citations (Scopus)

    Abstract

    Methylation of lysine 4 (K4) within histone H3 has been linked to active transcription and is removed by LSD1 and the JmjC domain-containing proteins by amino-oxidation or hydroxylation, respectively. Here, we describe the deamination catalyzed by Lysyl oxidase-like 2 protein (LOXL2) as an unconventional chemical mechanism for H3K4 modification. Infrared spectroscopy and mass spectrometry analyses demonstrated that recombinant LOXL2 specifically deaminates trimethylated H3K4. Moreover, LOXL2 activity is linked with the transcriptional control of . CDH1 gene by regulating H3K4me3 deamination. These results reveal another H3 modification and provide a different mechanism for H3K4 modification. © 2012 Elsevier Inc.
    Original languageEnglish
    Pages (from-to)369-376
    JournalMolecular Cell
    Volume46
    Issue number3
    DOIs
    Publication statusPublished - 11 May 2012

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