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Updated: Jun 21, 2026

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

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

Published on: August 4, 2019

Adaptive evolution of p53 thermodynamic stability.

Kian Hoe Khoo¹, Antonina Andreeva, Alan R Fersht

¹MRC Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, UK.

Journal of Molecular Biology

|August 18, 2009

Summary

Protein p53 stability varies across species, with vertebrates evolving lower thermodynamic stability linked to body temperature. Invertebrate p53 shows higher stability, suggesting adaptive evolution shapes this crucial tumor suppressor.

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Area of Science:

Protein biochemistry
Evolutionary biology
Molecular genetics

Background:

Protein thermodynamic stability is vital for evolution and adaptation.
The p53 tumor suppressor is crucial for gene regulation but often inactivated by mutations.
Human p53 exhibits low thermodynamic stability.

Purpose of the Study:

To investigate the thermodynamic and kinetic stability of p53 DNA binding domains across diverse species.
To understand the evolutionary pressures shaping p53 stability.
To correlate p53 stability with organismal body temperature.

Main Methods:

Differential scanning calorimetry (DSC) for thermal stability.
Equilibrium urea denaturation for unfolding.
Structure-guided mutagenesis on the human p53 scaffold.

Main Results:

Vertebrate p53 melting temperature correlates with body temperature.
p53 from homeotherm vertebrates has a short unfolding half-life (10-20 min) at body temperature.
Invertebrate p53 exhibits higher stability, similar to human p63 and p73.
Mutations on the p53 surface and interior enhance stability.

Conclusions:

Vertebrate p53 has evolved reduced thermodynamic stability and a short half-life, likely related to its function.
Adaptive evolution, driven by selective pressures, significantly impacts p53 DNA binding domain stability.
p53 stability is a dynamic trait shaped by evolutionary forces.