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Role of Jade-1 in the histone acetyltransferase (HAT) HBO1 complex.

Regulation of global chromatin acetylation is important for chromatin remodeling. A small family of Jade proteins includes Jade-1L, Jade-2, and Jade-3, each bearing two mid-molecule tandem plant homology domain (PHD) zinc fingers. We previously demonstrated that the short isoform of Jade-1L protein, Jade-1, is associated with endogenous histone acetyltransferase (HAT) activity. It has been found that Jade-1L/2/3 proteins co-purify with a novel HAT complex, consisting of HBO1, ING4/5, and Eaf6. We investigated a role for Jade-1/1L in the HBO1 complex. When overexpressed individually, neither Jade-1/1L nor HBO1 affected histone acetylation. However, co-expression of Jade-1/1L and HBO1 increased acetylation of the bulk of endogenous histone H4 in epithelial cells in a synergistic manner, suggesting that Jade1/1L positively regulates HBO1 HAT activity. Conversely, small interfering RNA-mediated depletion of endogenous Jade resulted in reduced levels of H4 acetylation. Moreover, HBO1-mediated H4 acetylation activity was enhanced severalfold by the presence of Jade-1/1L in vitro. The removal of PHD fingers affected neither binding nor mutual Jade-1-HBO1 stabilization but completely abrogated the synergistic Jade-1/1L- and HBO1-mediated histone H4 acetylation in live cells and in vitro with reconstituted oligonucleosome substrates. Therefore, PHDs are necessary for Jade-1/1L-induced acetylation of nucleosomal histones by HBO1. In contrast to Jade-1/1L, the PHD zinc finger protein ING4/5 failed to synergize with HBO1 to promote histone acetylation. The physical interaction of ING4/5 with HBO1 occurred in the presence of Jade-1L or Jade-3 but not with the Jade-1 short isoform. In summary, this study demonstrates that Jade-1/1L are crucial co-factors for HBO1-mediated histone H4 acetylation.

Pubmed ID: 18684714


  • Foy RL
  • Song IY
  • Chitalia VC
  • Cohen HT
  • Saksouk N
  • Cayrou C
  • Vaziri C
  • Côté J
  • Panchenko MV


The Journal of biological chemistry

Publication Data

October 24, 2008

Associated Grants

  • Agency: Canadian Institutes of Health Research, Id: 64289-2
  • Agency: Canadian Institutes of Health Research, Id: 87253-1
  • Agency: NCI NIH HHS, Id: R01 CA079830
  • Agency: NCI NIH HHS, Id: R01 CA79830
  • Agency: NIDDK NIH HHS, Id: R01 DK067569
  • Agency: NIDDK NIH HHS, Id: R01 DK087910
  • Agency: NIDDK NIH HHS, Id: R01 DK67569
  • Agency: NIEHS NIH HHS, Id: R01 ES12917

Mesh Terms

  • Cell Line
  • Cell Nucleus
  • Chromatin
  • Gene Expression Regulation
  • Gene Expression Regulation, Enzymologic
  • Genes, Reporter
  • Histone Acetyltransferases
  • Histones
  • Homeodomain Proteins
  • Humans
  • Models, Biological
  • Protein Isoforms
  • RNA, Small Interfering
  • Transfection
  • Tumor Suppressor Proteins