ArticleThe EMBO journal1992
Hsp104 is required for tolerance to many forms of stress.
Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 181 papers.
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Who cites it
181 citing papers in PubMed.
- Thermosensitivity of cellular translation restricts the growth of fission yeast at high temperatures.Communications biology · 2026Article
- High-throughput screening approach identifies substrate-selective Hsp104 variants that counter amyloid seeding with diminished off-target effects.Molecular cell · 2026Article
- Research progress on heat stress response mechanisms inFrontiers in microbiology · 2026Review
- Article
- Heat Shock Protein 104 (Genes · 2025Article
- HSP104 and HSP20-L Are Required by Aspergillus nidulans in Response to Attack by Fungivorous Springtail Sinella curviseta.Environmental microbiology reports · 2025Article
- Assays to measure small molecule Hsp70 agonist activity in vitro and in vivo.Analytical biochemistry · 2025Article
- Unveiling the genetic basis of the low pH response in the acidophilic yeast Maudiozyma bulderi as a potential host for biorefinery.FEMS yeast research · 2025Article
- Increased production of isobutanol from xylose through metabolic engineering of Saccharomyces cerevisiae overexpressing transcription factor Znf1 and exogenous genes.FEMS yeast research · 2024Article
- Nuclear Hsp104 safeguards the dormant translation machinery during quiescence.Nature communications · 2024Article
- Compatible solutes determine the heat resistance of conidia.Fungal biology and biotechnology · 2023Article
- Mechanisms of genotoxicity and proteotoxicity induced by the metalloids arsenic and antimony.Cellular and molecular life sciences : CMLS · 2023Review
- Tuning Hsp104 specificity to selectively detoxify α-synuclein.Molecular cell · 2023Article
- Overexpression of Hsp104 by Causing Dissolution of the Prion Seeds Cures the Yeast [International journal of molecular sciences · 2023Article
- MitoStores: chaperone-controlled protein granules store mitochondrial precursors in the cytosol.The EMBO journal · 2023Article
- Acute heat priming promotes short-term climate resilience of early life stages in a model sea anemone.PeerJ · 2023Article
- Enhancing the thermotolerance and erythritol production ofFrontiers in bioengineering and biotechnology · 2023Article
- Quiescence inAnnual review of genetics · 2022Review
- Clearance of an amyloid-like translational repressor is governed by 14-3-3 proteins.Cell reports · 2022Article
- Microbial adaptive evolution.Journal of industrial microbiology & biotechnology · 2022Review
121 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat-shock proteins (hsps) are induced by many types of stress. In Saccharomyces cerevisiae, a mutation in the HSP104 gene, a member of the highly conserved hsp100 gene family, reduces the ability of log-phase fermenting cells to withstand high temperatures after mild, conditioning pretreatments. Here, we examine the expression of hsp104 and its importance for survival under many different conditions. Hsp104 is expressed at a higher level in respiring cells than in fermenting cells and is required for the unusually high basal thermotolerance of respiring cells. Its expression in stationary phase cells and spores is crucial for the naturally high thermotolerance of these cell types and for their long-term viability at low temperatures. The protein is of critical importance in tolerance to ethanol and of moderate importance in tolerance to sodium arsenite. Thus, the hsp104 mutation establishes the validity of a long-standing hypothesis in the heat-shock field, namely, that hsps have broadly protective functions. Further, that a single protein is responsible for tolerance to heat, ethanol, arsenite and long-term storage in the cold indicates that the underlying causes of lethality are similar in an extraordinary variety of circumstances. Finally, the protein is of little or no importance in tolerance to copper and cadmium, suggesting that the lethal lesions produced by these agents are fundamentally different from those produced by heat.
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