Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment

Joaquin M. Espinosa, Beverly Emerson

Research output: Contribution to journalArticle

343 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)57-69
Number of pages13
JournalMolecular Cell
Volume8
Issue number1
DOIs
StatePublished - Jan 1 2001
Externally publishedYes

Fingerprint

Chromatin
Binding Sites
Tumor Suppressor Protein p53
Histone Acetyltransferases
TATA Box
Nucleosomes
DNA
DNA-Binding Proteins
Acetylation
Cell Cycle Checkpoints
Genes
Apoptosis

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment. / Espinosa, Joaquin M.; Emerson, Beverly.

In: Molecular Cell, Vol. 8, No. 1, 01.01.2001, p. 57-69.

Research output: Contribution to journalArticle

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