RETRACTED: Lysyl Oxidase-like 2 Deaminates Lysine 4 in Histone H3 (Retracted article. See vol. 63, pg. 180, 2016)

被引：65

作者：

Herranz, Nicolas ^{[1
,2
]}

Dave, Natalia ^{[1
]}

Millanes-Romero, Alba ^{[1
,2
]}

Morey, Lluis

Diaz, Victor M. ^{[1
,2
]}

Lorenz-Fonfria, Victor ^{[4
]}

Gutierrez-Gallego, Ricardo ^{[1
,2
]}

Jeronimo, Celia ^{[3
]}

Di Croce, Luciano ^{[3
,5
]}

Garcia de Herreros, Antonio ^{[1
,2
]}

Peiro, Sandra ^{[1
]}

机构：

[1] IMIM Hosp Mar, Programa Recerca Canc, Barcelona 08003, Spain

[2] Univ Pompeu Fabra, Dept Ciencies Expt & Salut, Barcelona 08003, Spain

[3] Ctr Regulacio Genom, Barcelona 08003, Spain

[4] Univ Autonoma Barcelona, Dept Bioquim & Biol Mol, Unitat Biofis, Barcelona 08003, Spain

[5] ICREA, Barcelona 08003, Spain

来源：

MOLECULAR CELL | 2012年 / 46卷 / 03期

关键词：

COMPLEX; DEMETHYLATION; METHYLATION; CHROMATIN; ENZYME; TRANSCRIPTION; DEACETYLASE; MECHANISMS; COMPONENT; SUBUNITS;

D O I：

10.1016/j.molcel.2012.03.002

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：369 / 376

页数：8

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