Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in histone H3
| Autor: | Víctor A. Lórenz-Fonfría, Natàlia Dave, Nicolás Herranz, Víctor M. Díaz, Antonio García de Herreros, Ane Iturbide, Luciano Di Croce, Laura Pascual-Reguant, Lluis Morey, Sandra Peiró, Alba Millanes-Romero, Ricardo Gutiérrez-Gallego, Célia Jeronimo |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Histone H3 Lysine 4 Spectrophotometry Infrared Lysine Blotting Western Lysyl oxidase Biology Biochemistry Methylation Cell Line Hydroxylation Histones 03 medical and health sciences chemistry.chemical_compound Histone H3 Antigens CD Cell Line Tumor Humans Molecular Biology LOXL2 Reverse Transcriptase Polymerase Chain Reaction Gene Expression Profiling Cell Biology Cadherins 030104 developmental biology chemistry Gene Expression Regulation Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization H3K4me3 RNA Interference Amino Acid Oxidoreductases Oxidation-Reduction |
| Zdroj: | The FEBS journal. 283(23) |
| ISSN: | 1742-4658 |
| Popis: | Methylation of histone H3 lysine 4 is linked to active transcription and can be removed by LSD1 or the JmjC domain-containing proteins by amino-oxidation or hydroxylation, respectively. Here we describe that its deamination can be catalyzed by lysyl oxidase-like 2 protein (LOXL2), presenting an unconventional chemical mechanism for H3K4 modification. Infrared spectroscopy and mass spectrometry analyses demonstrated that recombinant LOXL2 specifically deaminates trimethylated H3K4. Moreover, by regulating H3K4me3 deamination, LOXL2 activity is linked with the transcriptional control of the CDH1 gene. These results reveal the existence of further H3 modification as well as a novel mechanism for H3K4me3 demethylation. Database The GEO accession number for the data referred to this paper is GSE35600. |
| Databáze: | OpenAIRE |
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