ArticleProceedings of the National Academy of Sciences of the United States of America2002
Dynamic association of transcriptional activation domains and regulatory regions in Saccharomyces cerevisiae heat shock factor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 28 citations in OpenAlex.
- Thermotolerant yeasts promoting climate-resilient bioproduction.FEMS yeast research · 2025Review
- The conserved PBAF nucleosome-remodeling complex mediates the response to stress in Caenorhabditis elegans.Molecular and cellular biology · 2014Article
- Association of constitutive hyperphosphorylation of Hsf1p with a defective ethanol stress response in Saccharomyces cerevisiae sake yeast strains.Applied and environmental microbiology · 2012Article
- Orthologs of the class A4 heat shock transcription factor HsfA4a confer cadmium tolerance in wheat and rice.The Plant cell · 2009Article
- Specific interaction between tomato HsfA1 and HsfA2 creates hetero-oligomeric superactivator complexes for synergistic activation of heat stress gene expression.The Journal of biological chemistry · 2009Article
- The natural osmolyte trehalose is a positive regulator of the heat-induced activity of yeast heat shock transcription factor.Molecular and cellular biology · 2007Article
- De novo appearance and "strain" formation of yeast prion [PSI+] are regulated by the heat-shock transcription factor.Genetics · 2006Article
- A functional module of yeast mediator that governs the dynamic range of heat-shock gene expression.Genetics · 2006Article
- Genome-wide analysis of the biology of stress responses through heat shock transcription factor.Molecular and cellular biology · 2004Article
- Phosphorylation of the yeast heat shock transcription factor is implicated in gene-specific activation dependent on the architecture of the heat shock element.Molecular and cellular biology · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In Saccharomyces cerevisiae, the heat shock transcription factor (HSF) is thought to be a homotypic trimer that is bound to the promoters of heat shock protein (HSP) genes at both normal and heat shock temperatures. Exposure to heat shock greatly and rapidly induces HSF transcriptional activity without further increasing DNA-binding affinity. It is believed that HSF is under negative regulation at normal growth temperatures, but the detailed mechanism by which HSF is activated is still not clear. We report the analysis of mutations in a conserved arginine (residue 274) at the C-terminal end of the DNA-binding domain (DBD). Two mutations significantly increase both basal activity of HSF at normal temperatures and induced activity on heat shock. We demonstrate by coimmunoprecipitation experiments that the mutations reduce the association between the DNA-binding domain/oligomerization domain and the transcription activation domains. Our studies suggest that the DNA-binding domain of HSF can interact with activation domains directly, and this interaction is important for the repression of HSF activity under normal growth conditions. Destabilizing this interaction by heat or by mutations results in HSF transcriptional activation. We propose that Arg-274 is critical for intramolecular repression of HSF activity in normally growing cells.
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