The bromodomain of Gcn5 regulates site specificity of lysine acetylation on histone H3.

@article{Cieniewicz2014TheBO,
  title={The bromodomain of Gcn5 regulates site specificity of lysine acetylation on histone H3.},
  author={Anne M. Cieniewicz and Linley E. Moreland and Alison E Ringel and Samuel G. Mackintosh and Ana Raman and Tonya M Gilbert and Cynthia Wolberger and Alan J. Tackett and Sean D. Taverna},
  journal={Molecular & cellular proteomics : MCP},
  year={2014},
  volume={13 11},
  pages={2896-910}
}
In yeast, the conserved histone acetyltransferase (HAT) Gcn5 associates with Ada2 and Ada3 to form the catalytic module of the ADA and SAGA transcriptional coactivator complexes. Gcn5 also contains an acetyl-lysine binding bromodomain that has been implicated in regulating nucleosomal acetylation in vitro, as well as at gene promoters in cells. However, the contribution of the Gcn5 bromodomain in regulating site specificity of HAT activity remains unclear. Here, we used a combined acid-urea gel… CONTINUE READING
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