TY - JOUR
T1 - Lysyl Oxidase-like 2 Deaminates Lysine 4 in Histone H3
AU - Herranz, Nicolás
AU - Dave, Natàlia
AU - Millanes-Romero, Alba
AU - Morey, Lluis
AU - Díaz, Víctor M.
AU - Lórenz-Fonfría, Víctor
AU - Gutierrez-Gallego, Ricardo
AU - Jerónimo, Celia
AU - Di Croce, Luciano
AU - García de Herreros, Antonio
AU - Peiró, Sandra
PY - 2012/5/11
Y1 - 2012/5/11
N2 - 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.
AB - 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.
U2 - 10.1016/j.molcel.2012.03.002
DO - 10.1016/j.molcel.2012.03.002
M3 - Article
VL - 46
SP - 369
EP - 376
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 3
ER -