Literature DB >> 22483618

Lysyl oxidase-like 2 deaminates lysine 4 in histone H3.

Nicolás Herranz1, 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.   

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.
Copyright © 2012 Elsevier Inc. All rights reserved.

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Year:  2012        PMID： 22483618     DOI： 10.1016/j.molcel.2012.03.002

Source DB:  PubMed          Journal:  Mol Cell        ISSN： 1097-2765            Impact factor:   17.970


  33 in total

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