期刊
MOLECULAR CELL
卷 46, 期 3, 页码 369-376出版社
CELL PRESS
DOI: 10.1016/j.molcel.2012.03.002
关键词
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资金
- FIS [PS09/00258, CP08/00223]
- MEC [SAF2006-00339, SAF2010-16089]
- Fundacion Cientifica de la Asociacion Espanola contra el Cancer (AECC)
- Instituto Carlos III [RD06/0020/0040]
- Generalitat de Catalunya [2009SGR867]
- AECC
- EMBO
- CIHR
- ICREA Funding Source: Custom
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.
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