Abstract:
:The tumor suppressor protein, p53, plays a critical role in mediating cellular response to stress signals by regulating genes involved in cell cycle arrest and apoptosis. p53 is believed to be inactive for DNA binding unless its C terminus is modified or structurally altered. We show that unmodified p53 actively binds to two sites at -1.4 and -2.3 kb within the chromatin-assembled p21 promoter and requires the C terminus and the histone acetyltransferase, p300, for transcription. Acetylation of the C terminus by p300 is not necessary for binding or promoter activation. Instead, p300 acetylates p53-bound nucleosomes in the p21 promoter with spreading to the TATA box. Thus, p53 is an active DNA and chromatin binding protein that may selectively regulate its target genes by recruitment of specific cofactors to structurally distinct binding sites.
journal_name
Mol Celljournal_title
Molecular cellauthors
Espinosa JM,Emerson BMdoi
10.1016/s1097-2765(01)00283-0subject
Has Abstractpub_date
2001-07-01 00:00:00pages
57-69issue
1eissn
1097-2765issn
1097-4164pii
S1097-2765(01)00283-0journal_volume
8pub_type
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