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Breaking spore dormancy in budding yeast transforms the cytoplasm and the solubility of the proteome

New research from Plante et al. investigates the biophysical properties of the cytoplasm in yeast spores and their influence on cellular processes. Specifically, the study focuses on Saccharomyces cerevisiae spores, identifying that their cytoplasm is highly viscous and acidic during dormancy. Such conditions affect the solubility of over 100 proteins, including metabolic enzymes, which become more soluble as spores transition to active cell proliferation upon nutrient availability. Importantly, the heat shock protein Hsp42 plays a critical role in this transition, undergoing transient solubilization and phosphorylation, and is essential for the transformation of the cytoplasm during germination. The process of spore germination involves the dissolution of protein assemblies, a process partially orchestrated by Hsp42. The researchers suggest that these molecular property modulations in spores are likely key adaptations for their exceptional survival capabilities. This research utilized the IonOpticks Aurora Ultimate series.

Journal article – 2023 – Plos Biology


S. Plante; K.-M. Moon; P. Lemieux; L. J. Foster; C. R. Landry


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