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Pervasive Divergence in Protein Thermostability is Mediated by Both Structural Changes and Cellular Environments
Nilima Walunjkar1, Timothy Y Lai1, Nasima Akhter1
1Department of Biology, University of Rochester, Rochester, NY 14610, USA.
Molecular Biology and Evolution
|June 6, 2025
Summary
Organisms evolve thermotolerance through protein stability and cellular buffering. This study reveals that both protein structural changes and cellular context drive differences in protein thermostability between closely related Saccharomyces species.
Area of Science:
- Evolutionary biology
- Molecular biology
- Biochemistry
Background:
- Organisms possess diverse thermotolerance mechanisms, including protein stability and heat shock response systems.
- Thermophiles exhibit enhanced protein stability compared to mesophiles, suggesting its crucial role in heat adaptation.
- Understanding the molecular basis of thermotolerance is key to comprehending species adaptation to environmental constraints.
Purpose of the Study:
- To investigate the contributions of protein structural changes and cellular context to thermotolerance divergence between Saccharomyces cerevisiae and Saccharomyces uvarum.
- To quantify differences in protein thermostability between these two closely related species.
Main Methods:
- Thermal proteomic profiling was employed to assess protein melting temperatures.
- Interspecific hybrids were analyzed to evaluate the role of cellular context.
- Orthologous proteins were purified and characterized to identify underlying structural changes.
- Computational predictions were used to assess the impact of amino acid substitutions on protein stability.
Main Results:
- 85% of Saccharomyces cerevisiae proteins exhibited higher thermostability than their Saccharomyces uvarum homologs, with an average shift of 1.6 °C in melting temperature.
- Interspecific hybrids demonstrated that cellular context enhances the thermostability of Saccharomyces uvarum proteins.
- Amino acid substitutions were identified as the cause of melting temperature differences in specific proteins (Guk1, Aha1) and predicted to be widespread.
- Widespread changes in protein thermostability accompany the evolution of thermotolerance.
Conclusions:
- Both protein-level structural alterations and cellular environment significantly contribute to the evolution of thermotolerance.
- Divergence in protein thermostability between closely related species is driven by widespread amino acid substitutions.
- These findings provide insights into the molecular mechanisms underlying adaptation to thermal environments.
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