Molecular Cell
Volume 81, Issue 16, 19 August 2021, Pages 3294-3309.e12
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Article
Proteome plasticity in response to persistent environmental change

https://doi.org/10.1016/j.molcel.2021.06.028Get rights and content
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Highlights

  • Yeast responds to acute and persistent temperature shift differently

  • Persistent temperature shift induces alternative protein conformations

  • Fet3p adopts temperature-specific conformations, localizations, and functions

Summary

Temperature is a variable component of the environment, and all organisms must deal with or adapt to temperature change. Acute temperature change activates cellular stress responses, resulting in refolding or removal of damaged proteins. However, how organisms adapt to long-term temperature change remains largely unexplored. Here we report that budding yeast responds to long-term high temperature challenge by switching from chaperone induction to reduction of temperature-sensitive proteins and re-localizing a portion of its proteome. Surprisingly, we also find that many proteins adopt an alternative conformation. Using Fet3p as an example, we find that the temperature-dependent conformational difference is accompanied by distinct thermostability, subcellular localization, and, importantly, cellular functions. We postulate that, in addition to the known mechanisms of adaptation, conformational plasticity allows some polypeptides to acquire new biophysical properties and functions when environmental change endures.

Keywords

protein conformation changes
moonlighting functions
environmental stress
thermal acclimation
machine learning
Fet3

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These authors contributed equally

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