The PHD finger of p300 influences its ability to acetylate histone and non-histone targets.

@article{Rack2014ThePF,
  title={The PHD finger of p300 influences its ability to acetylate histone and non-histone targets.},
  author={Johannes Gregor Matthias Rack and Timo Lutter and Gro Elin Kj{\ae}reng Bjerga and Corina Guder and Christine Ehrhardt and Signe V{\"a}rv and Mathias Ziegler and Rein Aasland},
  journal={Journal of molecular biology},
  year={2014},
  volume={426 24},
  pages={3960-3972}
}
In enzymes that regulate chromatin structure, the combinatorial occurrence of modules that alter and recognise histone modifications is a recurrent feature. In this study, we explored the functional relationship between the acetyltransferase domain and the adjacent bromodomain/PHD finger (bromo/PHD) region of the transcriptional coactivator p300. We found that the bromo/PHD region of p300 can bind to the acetylated catalytic domain in vitro and augment the catalytic activity of the enzyme… CONTINUE READING
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