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

Journal article

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 sal...

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Authors: Arbely, E; Natan, E; Brandt, T; Allen, MD; Veprintsev, D

• Publication status: Published
• Journal: Proceedings of the National Academy of Sciences of the United States of America
• Volume: 108
• Issue: 20
• Pages: 8251-8256
• Publication date: 2011-05-01
• DOI: 10.1073/pnas.1105028108
• EISSN: 1091-6490
• ISSN: 0027-8424
• Language: English
• Keywords: Tumor Suppressor Protein p53; Lysine; Crystallography, X-Ray; Models, Molecular; DNA Damage; Binding Sites; Acetylation; Protein Engineering; Salts; DNA; Escherichia coli; Lysine-tRNA Ligase; Methanosarcina barkeri; Protein Structure, Tertiary