Journal Article10.1126/SCIENCE.2188365
HSP104 required for induced thermotolerance.
Yolanda Sánchez,Susan Lindquist +1 more
TL;DR: It is demonstrated that a particular heat shock protein plays a critical role in cell survival at extreme temperatures and is rescued with the wild-type gene.
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Abstract: A heat shock protein gene, HSP104, was isolated from Saccharomyces cerevisiae and a deletion mutation was introduced into yeast cells. Mutant cells grew at the same rate as wild-type cells and died at the same rate when exposed directly to high temperatures. However, when given a mild pre-heat treatment, the mutant cells did not acquire tolerance to heat, as did wild-type cells. Transformation with the wild-type gene rescued the defect of mutant cells. The results demonstrate that a particular heat shock protein plays a critical role in cell survival at extreme temperatures.
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Citations
Variations on a theme : combined molecular chaperone and proteolysis functions in Clp/HSP100 proteins.
TL;DR: The union of chaperone and proteolytic regulatory functions in one molecule suggests that certain Clp proteins play a decisive role in determining the destiny of proteins, not only during normal growth but also under conditions of extreme stress.
Engineered protein disaggregases mitigate toxicity of aberrant prion-like fusion proteins underlying sarcoma.
TL;DR: Yeast models of FUS-CHOP and EWS-FLI toxicity and aggregation are developed and Hsp104 variants might be employed to combat the toxicity and phase separation of aberrant fusion proteins involved in sarcoma.
Prion Propagation: The Role of Protein Dynamics
John A. Pezza,Tricia R. Serio +1 more
TL;DR: While the appearance, persistence and transfer of nucleic acid determinants require the synthesis of new polymers, recent studies indicate that prions are propagated through dynamic transitions in the structure of existing protein.
Hsp70 and a 54 kDa protein (Osp54) are induced in salmon (Salmo salar) in response to hyperosmotic stress.
TL;DR: The solute-specific and temporal patterns of response suggest that hsp70 and osp54 might function in concert to restore osmotic homeostasis and renature proteins destabilized or denatured during the early stages of osmosis shock.
Molecular determinants and modifiers of Matrin-3 toxicity, condensate dynamics, and droplet morphology
TL;DR: A yeast model of MATR3 proteotoxicity and aggregation was developed in this paper , where the authors used the Hsp104 variants to reverse this misfolding and demonstrate that these same variants also counter MATR 3 toxicity.
References
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The heat-shock proteins
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The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
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