Lysyl oxidase-like 2 deaminates lysine 4 in histone H3

Herranz Martín, Nicolás; Dave, Natàlia; Millanes Romero, Alba, 1986-; Morey Ramonell, Lluís; Díaz, Víctor M.; Lórenz Fonfria, Víctor; Gutiérrez Gallego, Ricardo, 1968-; Jerónimo, Celia; Di Croce, Luciano; García de Herreros, Antonio; Peiró Sales, Sandra

doi:http://dx.doi.org/10.1016/j.molcel.2012.03.002

Lysyl oxidase-like 2 deaminates lysine 4 in histone H3

Citation

Herranz N, Dave N, Millanes-Romero A, Morey L, Díaz VM, Lórenz-Fonfría V et al. Lysyl oxidase-like 2 deaminates lysine 4 in histone H3. Molecular cell. 2012;46(3):369-76. DOI: 10.1016/j.molcel.2012.03.002

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.