Journal of Bacteriology · 1993 · 125 citations · 31 references
Life SciencesGeneticsMolecular BiologyBioenergeticsGene ExpressionMicrobial GeneticsHeat Stress PhysiologyHeat Stress ToleranceTemperature ResponsesYeast BiologyYeast GeneticsGrowth RatesHeat Shock Response GenesSmall Heat Shock ProteinsTemperature-sensitive MutantsThermotolerance InductionVegetative Growth RegulationVegetative Growth SuppressionYeast Adaptation To Stress
The phenotypes of single Hsp104 and Hsp70 mutants of the budding yeast Saccharomyces cerevisiae provide no clue that these proteins are functionally related. Mutation of the HSP104 gene severely reduces the ability of cells to survive short exposures to extreme temperatures (thermotolerance) but has no effect on growth rates. On the other hand, mutations in the genes that encode Hsp70 proteins have significant effects on growth rates but do not reduce thermotolerance. The absence of a thermotolerance defect in S. cerevisiae Hsp70 mutants is puzzling, since the protein clearly plays an important role in thermotolerance in a variety of other organisms. In this report, examination of the phenotypes of combined Hsp104 and Hsp70 mutants uncovers similarities in the functions of Hsp104 and Hsp70 not previously apparent. In the absence of the Hsp104 protein, Hsp70 is very important for thermotolerance in S. cerevisiae, particularly at very early times after a temperature upshift. Similarly, Hsp104 plays a substantial role in vegetative growth under conditions of decreased Hsp70 protein levels. These results suggest a close functional relationship between Hsp104 and Hsp70.
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HSP104 Required for Induced Thermotolerance
Yolanda Sánchez, Susan Lindquist · Science · 1990 · 856 citations
Peptide-binding specificity of the molecular chaperone BiP
Gregory C. Flynn, Jan Pohl, Mark T. Flocco et al. · Nature · 1991 · 773 citations