ArticleNucleic acids research1998
Function of the C-terminal transactivation domain of human heat shock factor 2 is modulated by the adjacent negative regulatory segment.
Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Adaptation to heat stress by diversification of the vertebrate heat shock transcription factor family.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Heat shock transcription factors in development and disease.Disease models & mechanisms · 2026Review
- A guide to heat shock factors as multifunctional transcriptional regulators.The FEBS journal · 2025Review
- Article
- A novel mouse HSF3 has the potential to activate nonclassical heat-shock genes during heat shock.Molecular biology of the cell · 2010Article
- Stress-specific activation and repression of heat shock factors 1 and 2.Molecular and cellular biology · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA binding of heat shock factor 2 (HSF2) is induced during hemin-induced differentiation of human erythroleukemia cell line K562. To identify the transcriptional activation and the regulatory domains of HSF2, we constructed a series of deletion derivatives fused to the yeast GAL4 DNA binding domain and analyzed their transactivation activity. A minimal transactivation domain of HSF2 was localized to the C-terminus (residues 472-536), as in HSF1, although amino acid sequence similarity for these regions was rather limited and the potential transactivation ability was about 25% that of HSF1. The transactivation mediated by this region of HSF2 was found to be negatively regulated by the adjacent 18 amino acid segment (residues 428-445) under normal conditions. Furthermore, the latter segment, when fused to the GAL4 activation domain, markedly inhibited GAL4 activity. Extract containing most derivatives of HSF2 retaining this segment exhibited doublet or triplet bands in gel mobility shift assays with heat shock element-containing DNA, suggesting possible involvement of some factors interacting with that segment in the negative regulation. Another putative transactivation domain and two negative regulatory regions were also localized within the internal region.
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