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
Copper Activation of Superoxide Dismutase 1 (SOD1) in Vivo ROLE FOR PROTEIN-PROTEIN INTERACTIONS WITH THE COPPER CHAPERONE FOR SOD1
TL;DR: Yeast CCS was observed to insert copper into a pre-existing pool of apoSOD1 without the need for new SOD1 synthesis or for protein unfolding by the major SSA cytosolic heat shock proteins.
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The ATPase Activity of Hsp104, Effects of Environmental Conditions and Mutations
Eric C. Schirmer,Christine Queitsch,Anthony S. Kowal,Dawn A. Parsell,Susan Lindquist,Susan Lindquist +5 more
TL;DR: Either the functions of the two NBDs in ClpA and Hsp104 have been reversed or both contribute to ATP hydrolysis and oligomerization in a complex manner that can be idiosyncratically affected by such mutations.
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Characterization of the Stress Protein Response in Two Species of Collisella Limpets with Different Temperature Tolerances
TL;DR: Parts of the stress protein response may play a role in allowing C. scabra to tolerate the temperature extremes of the high intertidal region that provides it with access to food sources not available to closely related but more temperature-sensitive species.
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Analysis of the resistance to heat and hydrogen peroxide stresses in COS cells transiently expressing wild type or deletion mutants of the Drosophila 27-kDa heat-shock protein.
Patrick Mehlen,Jérôme Briolay,Leila Smith,Chantal Diaz-Latoud,Nathalie Fabre,Daniel Pauli,André-Patrick Arrigo +6 more
TL;DR: Biochemical fractionation and indirect immunofluorescence analysis indicated that the protective function of Dhsp27 was localized at the level of the nucleus, suggesting that the N-terminal half of the conserved alpha-crystallin domain may not be essential for the protective activity of the small hsp.
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Heat-shock proteins and stress tolerance in microorganisms.
TL;DR: Heat-shock proteins help microorganisms cope with the toxic effects of a wide variety of stresses and some help the organism grow under moderately stressful conditions, while others help it to survive more extreme conditions.
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