Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in histone H3

Nicolás Herranz; Natàlia Dave; Alba Millanes-Romero; Laura Pascual-Reguant; Lluis Morey; Víctor M. Díaz; Víctor Lórenz-Fonfría; Ricardo Gutierrez-Gallego; Celia Jerónimo; Ane Iturbide; Luciano Di Croce; Antonio García de Herreros; Sandra Peiró

doi:10.1111/febs.13922

Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in histone H3

Nicolás Herranz, Natàlia Dave, Alba Millanes-Romero, Laura Pascual-Reguant, Lluis Morey, Víctor M. Díaz, Víctor Lórenz-Fonfría, Ricardo Gutierrez-Gallego, Celia Jerónimo, Ane Iturbide, Luciano Di Croce, Antonio García de Herreros, Sandra Peiró

Research output: Contribution to journal › Article › Research › peer-review

23 Citations (Scopus)

Abstract

© 2016 Federation of European Biochemical Societies 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.

Original language	English
Pages (from-to)	4263-4273
Journal	FEBS Journal
Volume	283
Issue number	23
DOIs	https://doi.org/10.1111/febs.13922
Publication status	Published - 1 Dec 2016

Keywords

epigenetics
histone modification
lysyl oxidase-like 2
snail1
transcriptional regulation

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Herranz, Nicolás ; Dave, Natàlia ; Millanes-Romero, Alba ; Pascual-Reguant, Laura ; Morey, Lluis ; Díaz, Víctor M. ; Lórenz-Fonfría, Víctor ; Gutierrez-Gallego, Ricardo ; Jerónimo, Celia ; Iturbide, Ane ; Di Croce, Luciano ; García de Herreros, Antonio ; Peiró, Sandra. / Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in histone H3. In: FEBS Journal. 2016 ; Vol. 283, No. 23. pp. 4263-4273.

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title = "Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in histone H3",

abstract = "{\textcopyright} 2016 Federation of European Biochemical Societies 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.",

keywords = "epigenetics, histone modification, lysyl oxidase-like 2, snail1, transcriptional regulation",

author = "Nicol{\'a}s Herranz and Nat{\`a}lia Dave and Alba Millanes-Romero and Laura Pascual-Reguant and Lluis Morey and D{\'i}az, {V{\'i}ctor M.} and V{\'i}ctor L{\'o}renz-Fonfr{\'i}a and Ricardo Gutierrez-Gallego and Celia Jer{\'o}nimo and Ane Iturbide and {Di Croce}, Luciano and {Garc{\'i}a de Herreros}, Antonio and Sandra Peir{\'o}",

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Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in histone H3. / Herranz, Nicolás; Dave, Natàlia; Millanes-Romero, Alba; Pascual-Reguant, Laura; Morey, Lluis; Díaz, Víctor M.; Lórenz-Fonfría, Víctor; Gutierrez-Gallego, Ricardo; Jerónimo, Celia; Iturbide, Ane; Di Croce, Luciano; García de Herreros, Antonio; Peiró, Sandra.

In: FEBS Journal, Vol. 283, No. 23, 01.12.2016, p. 4263-4273.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in histone H3

AU - Herranz, Nicolás

AU - Dave, Natàlia

AU - Millanes-Romero, Alba

AU - Pascual-Reguant, Laura

AU - Morey, Lluis

AU - Díaz, Víctor M.

AU - Lórenz-Fonfría, Víctor

AU - Gutierrez-Gallego, Ricardo

AU - Jerónimo, Celia

AU - Iturbide, Ane

AU - Di Croce, Luciano

AU - García de Herreros, Antonio

AU - Peiró, Sandra

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AB - © 2016 Federation of European Biochemical Societies 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.

KW - epigenetics

KW - histone modification

KW - lysyl oxidase-like 2

KW - snail1

KW - transcriptional regulation

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