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Yeast As a Chassis for Developing Functional Assays to Study Human P53
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Structural Basis for p53 Lys120-Acetylation-Dependent DNA-Binding Mode.

Radion Vainer1, Sarit Cohen2, Anat Shahar3

  • 1Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva, 84105, Israel.

Journal of Molecular Biology
|June 25, 2016
PubMed
Summary

Acetylation of Lys120 in the tumor suppressor protein p53 enhances its DNA-binding specificity. This modification alters loop L1 conformation, enabling sequence-dependent binding and promoting proapoptotic gene transcription.

Keywords:
Hoogsteen base pairingapoptosisgenetic code expansionlysine acetylationtranscription

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Cellular homeostasis relies on precise gene expression control via transcription factors.
  • Mechanisms for transcription factor specificity in response to cellular signals are not fully understood.
  • Lysine 120 acetylation on tumor suppressor p53 promotes proapoptotic gene transcription.

Purpose of the Study:

  • To elucidate the structural basis of Lys120 acetylation's effect on p53 DNA-binding specificity.
  • To understand how p53 distinguishes between different DNA response elements.

Main Methods:

  • X-ray crystallography of Lys120-acetylated p53 DNA-binding domain.
  • Complex formation with consensus and BAX response elements.
  • Structural analysis of protein-DNA interactions.

Main Results:

  • Lys120 acetylation expands loop L1 conformational flexibility in the DNA-bound state.
  • Acetylation enables sequence-dependent DNA-binding modes for p53.
  • Binding to the BAX element induces global conformational changes, DNA deformation, and an asymmetric tetrameric complex.

Conclusions:

  • Lys120 acetylation of p53 is crucial for modulating its DNA-binding specificity.
  • Structural flexibility in loop L1, induced by acetylation, dictates sequence recognition.
  • A model for acetylation-dependent DNA-binding is proposed, impacting p53's role in gene regulation.