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Updated: Jul 11, 2026

Yeast As a Chassis for Developing Functional Assays to Study Human P53
14:57

Yeast As a Chassis for Developing Functional Assays to Study Human P53

Published on: August 4, 2019

Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain

W Gu1, R G Roeder

  • 1Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10021, USA.

Cell
|August 22, 1997
PubMed

Insights

The tumor suppressor p53 protein

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • The tumor suppressor p53 is a transcription factor crucial for inhibiting cell proliferation.
  • p53's antiproliferative function relies on its DNA-binding activity.
  • The regulation of p53's DNA binding is critical for its tumor suppressor role.

Purpose of the Study:

  • To investigate the post-translational modification of p53 by acetylation.
  • To determine the functional consequences of p53 acetylation on its DNA-binding activity.
  • To explore the role of p53 acetylation in the context of transcriptional coactivators.

Main Methods:

  • In vivo and in vitro acetylation assays of p53.
  • Identification of the specific acetylation site on p53.
  • Analysis of p53 DNA-binding activity following acetylation.

Main Results:

  • p53 undergoes acetylation both in vivo and in vitro.
  • Acetylation occurs at a C-terminal domain critical for p53 DNA binding.
  • Acetylation by p300 significantly enhances p53's sequence-specific DNA-binding activity.
  • Acetylation may induce a conformational change in p53, modulating its function.

Conclusions:

  • Acetylation represents a novel mechanism for activating p53 function.
  • This study provides evidence for acetylation-mediated functional changes in nonhistone regulatory proteins.
  • Findings have implications for understanding the mechanisms of acetyltransferase coactivators beyond histone modification.

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