ArticleProceedings of the National Academy of Sciences of the United States of America1996
Heat-shock protein 104 expression is sufficient for thermotolerance in yeast.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed, 225 citations in OpenAlex.
- Thermosensitivity of cellular translation restricts the growth of fission yeast at high temperatures.Communications biology · 2026Article
- Emerging fungal threats from the environment-a lesson from Candida auris and a warning about a second candidate, Rhodosporidiobolus fluvialis.PLoS pathogens · 2026Article
- A chaperone-proteasome-based fragmentation machinery is essential for aggrephagy.Nature cell biology · 2025Article
- rDNA copy number variation affects yeast fitness in response to different environments.Genetics · 2025Article
- Thermotolerant yeasts promoting climate-resilient bioproduction.FEMS yeast research · 2025Review
- The relationship mammalian p38 with human health and its homolog Hog1 in response to environmental stresses inFrontiers in cell and developmental biology · 2025Review
- Tuning Hsp104 specificity to selectively detoxify α-synuclein.Molecular cell · 2023Article
- Exploiting inter-tissue stress signaling mechanisms to preserve organismal proteostasis during aging.Frontiers in physiology · 2023Review
- Augmented peroxisomal ROS buffering capacity renders oxidative and thermal stress cross-tolerance in yeast.Microbial cell factories · 2021Article
- Meiosis-Based Laboratory Evolution of the Thermal Tolerance inFrontiers in bioengineering and biotechnology · 2021Article
- Differential proteomic analysis by SWATH-MS unravels the most dominant mechanisms underlying yeast adaptation to non-optimal temperatures under anaerobic conditions.Scientific reports · 2020Article
- The prion-like protein kinase Sky1 is required for efficient stress granule disassembly.Nature communications · 2019Article
- Review
- Engineering tolerance to industrially relevant stress factors in yeast cell factories.FEMS yeast research · 2017Review
- Protein aggregation in Ehrlichia chaffeensis during infection of mammalian cells.FEMS microbiology letters · 2017Article
- Hsp78 (78 kDa Heat Shock Protein), a Representative AAA Family Member Found in the Mitochondrial Matrix ofFrontiers in molecular biosciences · 2017Review
- Protein Quality Control by Molecular Chaperones in Neurodegeneration.Frontiers in neuroscience · 2017Review
- Absolute protein quantification of the yeast chaperome under conditions of heat shock.Proteomics · 2016Article
- Oxygen availability strongly affects chronological lifespan and thermotolerance in batch cultures ofMicrobial cell (Graz, Austria) · 2015Article
- Endothelial Thermotolerance Impairs Nanoparticle Transport in Tumors.Cancer research · 2015Article
18 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In all organisms, mild heat pretreatments induce tolerance to high temperatures. In the yeast Saccharomyces cerevisiae, such pretreatments strongly induce heat-shock protein (Hsp) 104, and hsp104 mutations greatly reduce high-temperature survival, indicating Hsp1O4 plays a critical role in induced thermotolerance. Surprisingly, however, a heat-shock transcription factor mutation (hsf1-m3) that blocks the induction of Hsps does not block induced thermotolerance. To resolve these apparent contradictions, we reexamined Hsp expression in hsf1-m3 cells. HsplO4 was expressed at a higher basal level in this strain than in other S. cerevisiae strains. Moreover, whereas the hsf1-m3 mutation completely blocked the induction of Hsp26 by heat, it did not block the induction of Hsp1O4. HSP104 could not be deleted in hsf1-m3 cells because the expression of heat-shock factor (and the viability of the strain) requires nonsense suppression mediated by the yeast prion [PSI+], which in turn depends upon Hsp1O4. To determine whether the level of Hsp1O4 expressed in hsf1-m3 cells is sufficient for thermotolerance, we used heterologous promoters to regulate Hsp1O4 expression in other strains. In the presence of other inducible factors (with a conditioning pretreatment), low levels of Hsp1O4 are sufficient to provide full thermotolerance. More remarkably, in the absence of other inducible factors (without a pretreatment), high levels of Hsp1O4 are sufficient. We conclude that Hsp1O4 plays a central role in ameliorating heat toxicity. Because Hsp1O4 is nontoxic and highly conserved, manipulating the expression of Hsp1OO proteins provides an excellent prospect for manipulating thermotolerance in other species.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.