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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56 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)369-376
Number of pages8
JournalMolecular Cell
Issue number3
StatePublished - May 11 2012

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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    Herranz, N., Dave, N., Millanes-Romero, A., Morey, L., Díaz, V. M., Lórenz-Fonfría, V., Gutierrez-Gallego, R., Jerónimo, C., Di Croce, L., García de Herreros, A., & Peiró, S. (2012). Lysyl Oxidase-like 2 Deaminates Lysine 4 in Histone H3. Molecular Cell, 46(3), 369-376.