Abstract:
:Cellular DNA damage causes stabilization and activation of the tumor suppressor and transcription factor p53, in part by promoting multiple covalent modifications of the p53 protein, including acetylation. We investigated the importance of acetylation in p53 function and the mechanism by which acetylation influences p53 activity. Acetylation site substitutions reduced p53-dependent transcriptional induction and G1 cell cycle arrest. Chromatin immunoprecipitation analysis of the endogenous p21 promoter showed increased association of p53, coactivators (CBP and TRRAP), and acetylated histones following cell irradiation. Results with acetylation-defective p53 demonstrate that the critical function of acetylation is not to increase the DNA binding affinity of p53 but rather to promote coactivator recruitment and histone acetylation. Therefore, we propose that an acetylation cascade consisting of p53 acetylation-dependent recruitment of coactivators/HATs is crucial for p53 function.
journal_name
Mol Celljournal_title
Molecular cellauthors
Barlev NA,Liu L,Chehab NH,Mansfield K,Harris KG,Halazonetis TD,Berger SLdoi
10.1016/s1097-2765(01)00414-2subject
Has Abstractpub_date
2001-12-01 00:00:00pages
1243-54issue
6eissn
1097-2765issn
1097-4164pii
S1097-2765(01)00414-2journal_volume
8pub_type
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