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Differential recognition of heat shock elements by members of the heat shock transcription factor family.
FEBS J. 2009 Apr; 276(7):1962-74.FJ

Abstract

Heat shock transcription factor (HSF), an evolutionarily conserved stress response regulator, forms trimers and binds to heat shock element (HSE), comprising at least three continuous inverted repeats of the sequence 5'-nGAAn-3'. The single HSF of yeast is also able to bind discontinuously arranged nGAAn units. We investigated interactions between three human HSFs and various HSE types in vitro, in yeast cells, and in HeLa cells. Human HSF1, a stress-activated regulator, preferentially bound to continuous HSEs rather than discontinuous HSEs, and heat shock of HeLa cells caused expression of reporter genes containing continuous HSEs. HSF2, whose function is implicated in neuronal specification and spermatogenesis, exhibited a slightly higher binding affinity to discontinuous HSEs than did HSF1. HSF4, a protein required for ocular lens development, efficiently recognized discontinuous HSEs in a trimerization-dependent manner. Among four human gamma-crystallin genes encoding structural proteins of the lens, heat-induced HSF1 preferred HSEs on the gammaA-crystallin and gammaB-crystallin promoters, whereas HSF4 preferred HSE on the gammaC-crystallin promoter. These results suggest that the HSE architecture is an important determinant of which HSF members regulate genes in diverse cellular processes.

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Authors+Show Affiliations

Yamamoto N
Department of Clinical Laboratory Science, Kanazawa University Graduate School of Medical Science, Kanazawa, Ishikawa, Japan.
Takemori Y
No affiliation info available
Sakurai M
No affiliation info available
Sugiyama K
No affiliation info available
Sakurai H
No affiliation info available

MeSH

Binding SitesDNA-Binding ProteinsHeLa CellsHeat Shock Transcription FactorsHeat-Shock ProteinsHeat-Shock ResponseHumansPhenotypePromoter Regions, GeneticRegulatory Elements, TranscriptionalSaccharomyces cerevisiaeTranscription Factorsgamma-Crystallins

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19250318

Citation

Yamamoto, Noritaka, et al. "Differential Recognition of Heat Shock Elements By Members of the Heat Shock Transcription Factor Family." The FEBS Journal, vol. 276, no. 7, 2009, pp. 1962-74.
Yamamoto N, Takemori Y, Sakurai M, et al. Differential recognition of heat shock elements by members of the heat shock transcription factor family. FEBS J. 2009;276(7):1962-74.
Yamamoto, N., Takemori, Y., Sakurai, M., Sugiyama, K., & Sakurai, H. (2009). Differential recognition of heat shock elements by members of the heat shock transcription factor family. The FEBS Journal, 276(7), 1962-74. https://doi.org/10.1111/j.1742-4658.2009.06923.x
Yamamoto N, et al. Differential Recognition of Heat Shock Elements By Members of the Heat Shock Transcription Factor Family. FEBS J. 2009;276(7):1962-74. PubMed PMID: 19250318.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Differential recognition of heat shock elements by members of the heat shock transcription factor family. AU - Yamamoto,Noritaka, AU - Takemori,Yukiko, AU - Sakurai,Mayumi, AU - Sugiyama,Kazuhisa, AU - Sakurai,Hiroshi, Y1 - 2009/02/23/ PY - 2009/3/3/entrez PY - 2009/3/3/pubmed PY - 2009/4/16/medline SP - 1962 EP - 74 JF - The FEBS journal JO - FEBS J VL - 276 IS - 7 N2 - Heat shock transcription factor (HSF), an evolutionarily conserved stress response regulator, forms trimers and binds to heat shock element (HSE), comprising at least three continuous inverted repeats of the sequence 5'-nGAAn-3'. The single HSF of yeast is also able to bind discontinuously arranged nGAAn units. We investigated interactions between three human HSFs and various HSE types in vitro, in yeast cells, and in HeLa cells. Human HSF1, a stress-activated regulator, preferentially bound to continuous HSEs rather than discontinuous HSEs, and heat shock of HeLa cells caused expression of reporter genes containing continuous HSEs. HSF2, whose function is implicated in neuronal specification and spermatogenesis, exhibited a slightly higher binding affinity to discontinuous HSEs than did HSF1. HSF4, a protein required for ocular lens development, efficiently recognized discontinuous HSEs in a trimerization-dependent manner. Among four human gamma-crystallin genes encoding structural proteins of the lens, heat-induced HSF1 preferred HSEs on the gammaA-crystallin and gammaB-crystallin promoters, whereas HSF4 preferred HSE on the gammaC-crystallin promoter. These results suggest that the HSE architecture is an important determinant of which HSF members regulate genes in diverse cellular processes. SN - 1742-4658 UR - https://www.unboundmedicine.com/medline/citation/19250318/Differential_recognition_of_heat_shock_elements_by_members_of_the_heat_shock_transcription_factor_family_ L2 - https://doi.org/10.1111/j.1742-4658.2009.06923.x DB - PRIME DP - Unbound Medicine ER -