Lysyl Oxidase-like 2 Deaminates Lysine 4 in Histone H3

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• 作者：Nicolá ; s Herranz¹ ; ² ; Natà ; lia Dave¹ ; Alba Millanes-Romero¹ ; ² ; Lluis Morey³ ; Ví ; ctor  ; M. Dí ; az¹ ; ² ; Ví ; ctor L&#243 ; renz-Fonfrí ; a⁴ ; Ricardo Gutierrez-Gallego¹ ; ² ; Celia Jer&#243 ; nimo³ ; Luciano Di  ; Croce³ ; ⁵ ; Antonio Garcí ; a  ; de  ; Herreros¹ ; ² ; Sandra Peir&#243 ; ¹ ; ^{speiro@imim.es}
• 刊名：Molecular Cell
• 出版年：2012
• 期刊代码：111_10972765
• 类别：bio
• 出版时间：11 May, 2012
• 卷：46
• 期：3
• 页码：369-376
• 文件大小：1002 K

摘要

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Summary

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.