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Titolo:
The loop domain of heat shock transcription factor 1 dictates DNA-binding specificity and responses to heat stress
Autore:
Ahn, SG; Liu, PCC; Klyachko, K; Morimoto, RI; Thiele, DJ;
Indirizzi:
Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 t Biol Chem, Ann Arbor, MI 48109 USA Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA Northwestern Univ Evanston IL USA 60208 Cell Biol, Evanston, IL 60208 USA
Titolo Testata:
GENES & DEVELOPMENT
fascicolo: 16, volume: 15, anno: 2001,
pagine: 2134 - 2145
SICI:
0890-9369(20010815)15:16<2134:TLDOHS>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
HELIX-TURN-HELIX; COILED-COIL; SACCHAROMYCES-CEREVISIAE; FACTOR TRIMERIZATION; PROTEIN-SYNTHESIS; GENE-EXPRESSION; FACTOR-II; IN-VIVO; HSF1; ACTIVATION;
Keywords:
HSF; HSP70; stress response; apoptosis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Thiele, DJ Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 48109 USAUniv Michigan Ann Arbor MI USA 48109 , Ann Arbor, MI 48109 USA
Citazione:
S.G. Ahn et al., "The loop domain of heat shock transcription factor 1 dictates DNA-binding specificity and responses to heat stress", GENE DEV, 15(16), 2001, pp. 2134-2145

Abstract

Eukaryotic heat shock transcription factors (HSF) regulate an evolutionarily conserved stress-response pathway essential for survival against a variety of environmental and developmental stresses. Although the highly similarHSF family members have distinct roles in responding to stress and activating target gene expression, the mechanisms that govern these roles are unknown. Here we identify a loop within the HSF1 DNA-binding domain that dictates HSF isoform specific DNA binding in vitro and preferential target gene activation by HSF family members in both a yeast transcription assay and in mammalian cells. These characteristics of the HSF1 loop region are transposable to HSF2 and sufficient to confer DNA-binding specificity, heat shock inducible HSP gene expression and protection from heat-induced apoptosis in vivo. In addition, the loop suppresses formation of the HSF1 trimer under basal conditions and is required for heat-inducible trimerization in a purified system in vitro, suggesting that this domain is a critical part of the HSF1 heat-stress-sensing mechanism. We propose that this domain defines a signature for HSF1 that constitutes an important determinant for how cells utilize a family of transcription factors to respond to distinct stresses.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 19:31:17