Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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HIF-1-Dependent Induction of Jumonji Domain-Containing Protein (JMJD) 3 under Hypoxic Conditions

  • Lee, Ho-Youl (Department of Life Science, University of Seoul) ;
  • Choi, Kang (Department of Life Science, University of Seoul) ;
  • Oh, Hookeun (Department of Life Science, University of Seoul) ;
  • Park, Young-Kwon (Department of Life Science, University of Seoul) ;
  • Park, Hyunsung (Department of Life Science, University of Seoul)
  • Received : 2013.09.06
  • Accepted : 2013.11.18
  • Published : 2014.01.31
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Abstract

Jumonji domain-containing proteins (JMJD) catalyze the oxidative demethylation of a methylated lysine residue of histones by using $O_2$, ${\alpha}$-ketoglutarate, vitamin C, and Fe(II). Several JMJDs are induced by hypoxic stress to compensate their presumed reduction in catalytic activity under hypoxia. In this study, we showed that an H3K27me3 specific histone demethylase, JMJD3 was induced by hypoxia-inducible factor (HIF)-$1{\alpha}/{\beta}$ under hypoxia and that treatment with Clioquinol, a HIF-$1{\alpha}$ activator, increased JMJD3 expression even under normoxia. Chromatin immunoprecipitation (ChIP) analyses showed that both HIF-$1{\alpha}$ and its dimerization partner HIF-$1{\beta}$/Arnt occupied the first intron region of the mouse JMJD3 gene, whereas the HIF-$1{\alpha}/{\beta}$ heterodimer bound to the upstream region of the human JMJD3, indicating that human and mouse JMJD3 have hypoxia-responsive regulatory regions in different locations. This study shows that both mouse and human JMJD3 are induced by HIF-1.

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References

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