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Data from: An adaptive biomolecular condensation response is conserved across environmentally divergent species

Keyport Kik, Samantha1; Christopher, Dana1; Glauninger, Hendrik1; Wong Hickernell, Caitlin1; Bard, Jared1; Lin, Kyle1; Ford, Michael2; Squires, Allison1; Sosnick, Tobin1; Drummond, D. Allan1

Published Aug 22, 2023; Updated Jan 11, 2024 on Dryad. https://doi.org/10.5061/dryad.w3r2280w6

Data files

Aug 22, 2023 version files 231.13 MB
Jan 11, 2024 version files 241.83 MB

Abstract

Cells must sense and respond to sudden maladaptive environmental changes—stresses—to survive and thrive. Across eukaryotes, stresses such as heat shock trigger conserved responses: growth arrest, a specific transcriptional response, and biomolecular condensation of protein and mRNA into structures known as stress granules under severe stress. The composition, formation mechanism, adaptive significance, and even evolutionary conservation of these condensed structures remain enigmatic. Here we provide an unprecedented view into stress-triggered condensation, its evolutionary conservation and tuning, and its integration into other well-studied aspects of the stress response. Using three morphologically near-identical budding yeast species adapted to different thermal environments and diverged by up to 100 million years, we show that proteome-scale biomolecular condensation is tuned to species-specific thermal niches, closely tracking corresponding growth and transcriptional responses. In each species, poly(A)-binding protein—a core marker of stress granules—condenses in isolation at species-specific temperatures, with conserved molecular features and conformational changes modulating condensation. From the ecological to the molecular scale, our results reveal previously unappreciated levels of evolutionary selection in the eukaryotic stress response, while establishing a rich, tractable system for further inquiry.