Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans.

Schuetz, Thomas; Gallo, G J; Sheldon, Lynn A.; Tempst, Paul; Kingston, Robert E.

doi:10.1073/pnas.88.16.6911

Cited by 328 publications

(253 citation statements)

References 32 publications

(36 reference statements)

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“…A fourth zipper motif is located at the COOH termini of all HSF molecules that have heat-inducible HSE-binding ability (8,14,41,45,46). This COOH-terminal hydrophobic heptad repeat has been postulated to play a role in regulating the HSE-binding activity of HSF (8).…”

Section: Resultsmentioning

confidence: 99%

The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70.

Mosser¹,

Duchaine²,

Massie³

1993

Mol. Cell. Biol.

187

130

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The human heat shock transcription factor (HSF) is maintained in an inactive non-DNA-binding form under nonstress conditions and acquires the ability to bind specifically to the heat shock promoter element in response to elevated temperatures or other conditions that disrupt protein structure. Here we show that constitutive overexpression of the major inducible heat shock protein, hsp7O, in transfected human cells reduces the extent of HSF activation after a heat stress. HSF activation was inhibited more strongly in clones that express higher levels of hsp7O. These results demonstrate that HSF activity is negatively regulated in vivo by hsp7O and suggest that the cell might sense elevated temperature as a decreased availability of hsp7O. HSF activation in response to treatment with sodium arsenite or the proline analog azetidine was also depressed in hsp7O-expressing cells relative to that in the nontransfected control cells. As well, the level of activated HSF decreased more rapidly in the hsp7O-expressing clones when the cells were heat shocked and returned to 37°C. These results suggest that hsp7O could play an active role in the conversion of HSF back to a conformation that does not bind the heat shock promoter element during the attenuation of the heat shock response.

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Section: Resultsmentioning

confidence: 99%

The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70.

Mosser¹,

Duchaine²,

Massie³

1993

Mol. Cell. Biol.

187

130

View full text Add to dashboard Cite

show abstract

“…The heat shock element serves as binding site for a family of transcription factors, referred to as heat shock transcription factors (HSF) (for review see: Morimoto et al, 1992;Lis and Wu, 1993). Three members of this family, HSF-1, HSF-2 and HSF-3, have been described in vertebrates (Rabindran et al, 1991;Sarge et al, 1991;Schuetz et al, 1991;Nakai and Morimoto. 1993).…”

Section: B-myb Activates the Hsp70 Promoter Via The Heat Shock Elementmentioning

confidence: 99%

B-Myb and cyclin D1 mediate heat shock element dependent activation of the human HSP70 promoter

Kamano

Klempnauer

1997

Oncogene

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Previous studies have shown that B-Myb, a conserved member of the Myb transcription factor family, is a potent activator of the promoter of the human HSP70 gene but does not activate promoters containing Myb binding sites. We have now investigated the transactivation properties of B-Myb in more detail. We here report that B-Myb activates the HSP70 promoter by a novel mechanism which involves the heat shock element (HSE). Deletion analysis of B-Myb shows that a speci®c domain in the center of B-Myb, but not the DNA-binding domain is required for HSE-dependent transactivation. We also show that deletion of the C-terminal domain of B-Myb does not a ect HSE-dependent transactivation but allows the protein to activate a promoter containing Myb binding sites. This suggests that the ability to activate Myb binding site containing promoters is repressed in the context of full length B-Myb and that HSE dependent and Myb binding site dependent transactivation are distinct functions of B-Myb. Finally, we report that cyclin D1 like B-Myb strongly activates the HSP70 promoter via the HSE. HSE-dependent transactivation is a novel activity of cyclin D1 and appears to be independent of the phosphorylation of the Rb protein. Our results reveal an interesting and unexpected connection between HSE-dependent gene activation and proteins expressed during the G1/Stransition of the cell cycle.

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“…Many hsps were identified in yeast cells, and some of the respective genes have been cloned. Some of these genes are highly homologous to each other and form subfam- (14,21,30,52,60,61,70,82). The HSF acts as a multimer (50,53,81) and in most organisms binds the HSE only upon heat shock (36,67,68).…”

mentioning

confidence: 99%

The yeast and mammalian Ras pathways control transcription of heat shock genes independently of heat shock transcription factor.

Engelberg¹,

Zandi²,

Parker³

et al. 1994

Mol. Cell. Biol.

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Yeast strains in which the Ras-cyclic AMP (cAMP) pathway is constitutively active are sensitive to heat shock, whereas mutants in which the activity of this pathway is low are hyperresistant to heat shock. To determine the molecular basis for these differences, we examined the transcriptional induction of heat shock genes in various yeast strains. Activation of heat shock genes was attenuated in the strains in which the Ras-cAMP pathway is constitutively active. In contrast, in a strain deficient in cAMP production, several heat shock genes were induced by removal of cAMP from the medium. These results indicate that the Ras-cAMP pathway affects the induction of heat shock genes. In all of the mutants, heat shock transcription factor expression and activity were identical to those in wild-type cells. The response to heat shock in Ha-rastransformed rat fibroblasts was also studied. While no induction of Hsp68 was observed in Ha-ras-transformed cells, proper regulation of heat shock transcription factor was found. Therefore, in mammals, as in Saccharomyces cerevisiae, the Ras pathway controls the transcription of heat shock genes via a mechanism not involving the heat shock transcription factor.The ras proto-oncogenes are highly conserved from yeasts to humans (reviewed in reference 12). These genes encode small membrane-associated GTP binding proteins that transduce signals generated at the cell surface to intracellular effectors (3,7,24,59). The mammalian Ha-Ras protein seems to interact with the serine or threonine kinase [77][78][79]85) and somehow leads to its activation. This results in activation of a protein kinase cascade (18,73,83) that induces gene expression through phosphorylation of transcription factors (reviewed in reference 25). One transcription factor affected by Ha-Ras is c-Jun (6), and another is NF-KB (17). In addition to positive modulation of the transcription factors' activity, HaRas may also negatively regulate certain transcription factors.In the yeast Saccharomyces cerevisiae, It was shown that expression of heat shock proteins (hsps) under nonshock conditions confers hyperresistance to heat shock (27,42,56). Therefore, it seems reasonable that resistance and sensitivity to heat shock are mediated at the level of hsp gene transcription. Indeed, it was shown that cyri cells express three proteins with a molecular mass of 72 kDa (65). These proteins, which were probably hsps, were not induced in the bcyl strain (65). Other studies showed that one of the heat shock genes, SSA3, was activated in the cyril strain in the absence of heat shock (9, 80). Also, the UBI4 gene, coding for polyubiquitin, was found to be regulated both by heat shock and cAMP (72). It is still not known, however, whether the Ras-cAMP pathway is a general regulator of hsp gene expression. It is also not known whether mammalian Ha-Ras activation also affects hsp gene expression. Furthermore, both in yeasts and in mammals, the relationship between the Ras pathway and the heat shock transcription factor (HSF [described bel...

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Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans.

Abstract: The heat shock response is transcriptionally regulated by an evolutionarily conserved protein termed heat shock factor (HSF). We report the purification to homogeneity and the partial peptide sequence of HSF from HeLa cells.

Cited by 328 publications

References 32 publications

The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70.

The DNA-binding activity of the human heat shock transcription factor is regulated in vivo by hsp70.

B-Myb and cyclin D1 mediate heat shock element dependent activation of the human HSP70 promoter

The yeast and mammalian Ras pathways control transcription of heat shock genes independently of heat shock transcription factor.

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