Pervasive Divergence in Protein Thermostability is Mediated by Both Structural Changes and Cellular Environments.

ABSTRACT: Temperature is a universal environmental constraint and organisms have evolved diverse mechanisms of thermotolerance. A central feature of thermophiles relative to mesophiles is a universal shift in protein stability, implying that it is a major constituent of thermotolerance. However, organisms have also evolved extensive buffering systems, such as those that disaggregate and refold denatured proteins and enable survival of heat shock. Here, we show that both cellular and protein structural changes contribute to divergence in protein thermostability between two closely related Saccharomyces species that differ by 8 °C in their thermotolerance. Using thermal proteomic profiling we find that 85% of S. cerevisiae proteins are more stable than their S. uvarum homologs and there is a 1.6 °C sh

SUBMITTER: Walunjkar N 

PROVIDER: S-EPMC12227239 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature