Premium
hADA3 is required for p53 activity
Author(s) -
Wang Ting,
Kobayashi Takahiko,
Takimoto Rishu,
Denes Alec E.,
Snyder Eric L.,
elDeiry Wafik S.,
Brachmann Rainer K.
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.22.6404
Subject(s) - biology , histone acetyltransferase , dna damage , transcription factor , microbiology and biotechnology , phosphorylation , histone , apoptosis , acetyltransferase , cell cycle checkpoint , dna , cell cycle , acetylation , p53 protein , suppressor , dna repair , transcription (linguistics) , genetics , gene , linguistics , philosophy
The tumor suppressor protein p53 is a transcription factor that is frequently mutated in human cancers. In response to DNA damage, p53 protein is stabilized and activated by post‐translational modifications that enable it to induce either apoptosis or cell cycle arrest. Using a novel yeast p53 dissociator assay, we identify hADA3, a part of histone acetyltransferase complexes, as an important cofactor for p53 activity. p53 and hADA3 physically interact in human cells. This interaction is enhanced dramatically after DNA damage due to phosphorylation event(s) in the p53 N‐terminus. Proper hADA3 function is essential for full transcriptional activity of p53 and p53‐mediated apoptosis.