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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

Effects of oncogenic mutations and DNA response elements on the binding of p53 to p53-binding protein 2 (53BP2)

Henning Tidow1, Dmitry B Veprintsev, Stefan M V Freund

  • 1Centre for Protein Engineering, Medical Research Council, Hills Road, Cambridge CB2 2QH, United Kingdom.

The Journal of Biological Chemistry
|August 5, 2006
PubMed

Insights

ASPP2 enhances p53

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Biophysics

Background:

  • The tumor suppressor p53 is crucial in cancer, inducing cell cycle arrest or apoptosis.
  • ASPP2 specifically enhances p53's apoptotic function, but the mechanism is unclear.

Purpose of the Study:

  • To investigate the mechanism by which ASPP2 selectively enhances p53's pro-apoptotic activity.
  • To analyze the binding interactions between 53BP2, p53 core domain, and DNA response elements.

Main Methods:

  • Biophysical techniques were used to study the binding of 53BP2 to p53 core domain and mutants.
  • Analysis of p53 binding to DNA response elements (GADD45, p21, Bax, PIG3) in the presence of 53BP2.

Main Results:

  • p53 core domain mutations differentially affect 53BP2 and DNA binding.
  • 53BP2 binding to p53 is mutually exclusive with DNA binding for both pro-apoptotic and non-apoptotic response elements.
  • No evidence of a ternary complex involving 53BP2, p53, and DNA was observed.

Conclusions:

  • ASPP2 (via 53BP2) does not form a ternary complex with p53 and DNA.
  • The mechanism of ASPP2's selective enhancement of p53's apoptotic function likely involves competition for p53 binding sites rather than a ternary complex formation.

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