ArticleNucleic acids research2001
The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity.
Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 48 citations in OpenAlex.
- Genome-wide identification, classification and expression analysis of the heat shock transcription factor family in Garlic (Allium sativum L.).BMC plant biology · 2024Article
- PbHsfC1a-coordinates ABA biosynthesis and HPlant biotechnology journal · 2024Article
- SCHIZORIZA domain-function analysis identifies requirements for its specific role in cell fate segregation.Plant physiology · 2023Article
- Structures of heat shock factor trimers bound to DNA.iScience · 2021Article
- Genome-wide identification and analysis of the heat shock transcription factor family in moso bamboo (Phyllostachys edulis).Scientific reports · 2021Article
- Genome-Wide Investigation of Heat Shock Transcription Factor Family in Wheat (International journal of molecular sciences · 2020Article
- Article
- Genome-wide analysis identifies chickpea (Cicer arietinum) heat stress transcription factors (Hsfs) responsive to heat stress at the pod development stage.Journal of plant research · 2018Article
- Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Microbiology and molecular biology reviews : MMBR · 2012Review
- Cloning and characterization of HsfA2 from Lily (Lilium longiflorum).Plant cell reports · 2010Article
- Inhibition of DNA binding by differential sumoylation of heat shock factors.Molecular and cellular biology · 2006Article
- Heat stress response in plants: a complex game with chaperones and more than twenty heat stress transcription factors.Journal of biosciences · 2004Review
- Architecture of a fur binding site: a comparative analysis.Journal of bacteriology · 2003Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The yeast heat shock transcription factor (HSF) belongs to the winged helix family of proteins. HSF binds DNA as a trimer, and additional trimers can bind DNA co-operatively. Unlike other winged helix-turn-helix proteins, HSF's wing does not appear to contact DNA, as based on a previously solved crystal structure. Instead, the structure implies that the wing is involved in protein-protein interactions, possibly within a trimer or between adjacent trimers. To understand the function of the wing in the HSF DNA-binding domain, a Saccharomyces cerevisiae strain was created that expresses a wingless HSF protein. This strain grows normally at 30 degrees C, but shows a decrease in reporter gene expression during constitutive and heat-shocked conditions. Removal of the wing does not affect the stability or trimeric nature of a protein fragment containing the DNA-binding and trimerization domains. Removal of the wing does result in a decrease in DNA-binding affinity. This defect was mainly observed in the ability to form the first trimer-bound complex, as the formation of larger complexes is unaffected by the deletion. Our results suggest that the wing is not involved in the highly co-operative nature of HSF binding, but may be important in stabilizing the first trimer bound to DNA.
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