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Nucleosomes specify co-factor access to p53.

Deyasini Chakraborty1, Colby R Sandate2, Luke Isbel3

  • 1Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland; University of Basel, Basel, Switzerland.

Molecular Cell
|July 27, 2025
PubMed
Summary
This summary is machine-generated.

Chromatin structure dictates which co-factors can interact with the transcription factor p53. Nucleosome engagement creates a selective barrier, impacting DNA damage response and cell cycle regulation.

Keywords:
genome regulationtranscriptiontranscription co-factors

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Area of Science:

  • Molecular Biology
  • Chromatin Biology
  • Biochemistry

Background:

  • Pioneer transcription factors (TFs) bind DNA motifs within chromatin.
  • Understanding how TFs bound to nucleosomes interact with co-factors is crucial.
  • The p53 TF regulates critical cellular processes but often binds inaccessible chromatin.

Purpose of the Study:

  • To investigate the interaction of chromatin-bound p53 with co-factors from the ubiquitin proteasome system (UPS).
  • To determine how nucleosome engagement affects co-factor binding to p53.

Main Methods:

  • In vitro binding assays.
  • Cellular assays.
  • Cryo-electron microscopy (cryo-EM) structure determination.

Main Results:

  • The E3 ubiquitin ligase E6-E6AP could not bind nucleosome-engaged p53 at specific super-helical locations (SHL).
  • The deubiquitinase USP7 successfully engaged nucleosome-bound p53 both in vitro and in cells.
  • A cryo-EM structure revealed USP7 bound to p53 and nucleosomes.

Conclusions:

  • Chromatin acts as a selective barrier for p53 co-factor interactions.
  • The compatibility of co-factors, TFs, and chromatin is governed by flexible interaction domains.