4.8 Article Retracted Publication

被撤回的出版物: Lysyl Oxidase-like 2 Deaminates Lysine 4 in Histone H3 (Retracted article. See vol. 63, pg. 180, 2016)

期刊

MOLECULAR CELL
卷 46, 期 3, 页码 369-376

出版社

CELL PRESS
DOI: 10.1016/j.molcel.2012.03.002

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资金

  1. FIS [PS09/00258, CP08/00223]
  2. MEC [SAF2006-00339, SAF2010-16089]
  3. Fundacion Cientifica de la Asociacion Espanola contra el Cancer (AECC)
  4. Instituto Carlos III [RD06/0020/0040]
  5. Generalitat de Catalunya [2009SGR867]
  6. AECC
  7. EMBO
  8. CIHR
  9. ICREA Funding Source: Custom

向作者/读者索取更多资源

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.

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