Acetylation of lysine 120 of p53 endows DNA-binding specificity at effective physiological salt concentration.

@article{Arbely2011AcetylationOL,
  title={Acetylation of lysine 120 of p53 endows DNA-binding specificity at effective physiological salt concentration.},
  author={Eyal Arbely and Eviatar Natan and Tobias Brandt and Mark D. Allen and Dmitry B. Veprintsev and Carol V Robinson and Jason W Chin and Andreas C. Joerger and A. R. Fersht},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 20},
  pages={8251-6}
}
Lys120 in the DNA-binding domain (DBD) of p53 becomes acetylated in response to DNA damage. But, the role and effects of acetylation are obscure. We prepared p53 specifically acetylated at Lys120, AcK120p53, by in vivo incorporation of acetylated lysine to study biophysical and structural consequences of acetylation that may shed light on its biological role. Acetylation had no affect on the overall crystal structure of the DBD at 1.9-Å resolution, but significantly altered the effects of salt… CONTINUE READING

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Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA

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