Lysyl Oxidase-like 2 Deaminates Lysine 4 in Histone H3

Nicolás Herranz; 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

doi:10.1016/j.molcel.2012.03.002

Lysyl Oxidase-like 2 Deaminates Lysine 4 in Histone H3

Nicolás Herranz, 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

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

57 Citations (Scopus)

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. © 2012 Elsevier Inc.

Original language	English
Pages (from-to)	369-376
Journal	Molecular Cell
Volume	46
Issue number	3
DOIs	https://doi.org/10.1016/j.molcel.2012.03.002
Publication status	Published - 11 May 2012

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@article{32a49092abd641d1ae3ce1f2af4f813a,

title = "Lysyl Oxidase-like 2 Deaminates Lysine 4 in Histone H3",

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. {\textcopyright} 2012 Elsevier Inc.",

author = "Nicol{\'a}s Herranz and Nat{\`a}lia Dave and Alba Millanes-Romero 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 {Di Croce}, Luciano and {Garc{\'i}a de Herreros}, Antonio and Sandra Peir{\'o}",

year = "2012",

month = may,

day = "11",

doi = "10.1016/j.molcel.2012.03.002",

language = "English",

volume = "46",

pages = "369--376",

journal = "Molecular Cell",

issn = "1097-2765",

publisher = "Cell Press",

number = "3",

}

Lysyl Oxidase-like 2 Deaminates Lysine 4 in Histone H3. / Herranz, Nicolás; Dave, Natàlia; Millanes-Romero, Alba; Morey, Lluis; Díaz, Víctor M.; Lórenz-Fonfría, Víctor; Gutierrez-Gallego, Ricardo; Jerónimo, Celia; Di Croce, Luciano; García de Herreros, Antonio; Peiró, Sandra.

In: Molecular Cell, Vol. 46, No. 3, 11.05.2012, p. 369-376.

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

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 -