Heat shock factor is required for growth at normal temperatures in the fission yeast Schizosaccharomyces pombe.

Gallo, G J; Prentice, Holly; Kingston, Robert E.

doi:10.1128/mcb.13.2.749

Cited by 85 publications

(73 citation statements)

References 49 publications

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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

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“…In yeast, HSF forms a trimer in solution and also binds DNA in this form (Sorger & Nelson, 1989). HSF is constitutively bound to DNA and acts as a transcription factor even under nonstressed conditions (Jakobsen & Pelham, 1988;Sorger & Pelham, 1988;Wiederrecht et al, 1988;Park & Craig, 1989;Gross et al, 1990;Chen & Pederson, 1993;Gallo et al, 1993). Heat shock conditions induce a higher level of transcriptional activation mediated by HSF through mechanisms that are not yet clear (Nieto-Sotelo et al, 1990;Sorger, 1990; Solution structure of heat shock factor Jakobsen & Pelham, 1991;Gallo et al, 1993).…”

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confidence: 99%

Solution structure of the DNA‐binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy

et al. 1994

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The solution structure of the 92-residue DNA-binding domain of the heat shock transcription factor from Kluyveromyces fuctis has been determined using multidimensional NMR methods. Three-dimensional (3D) triple resonance, 'H-'3C-'3C-'H total correlation spectroscopy, and I5N-separated total correlation spectroscopyheteronuclear multiple quantum correlation experiments were used along with various 2D spectra to make nearly complete assignments for the backbone and side-chain 'H, "N, and I3C resonances. Five-hundred eighty-three NOE constraints identified in 3D I3C-and "N-separated NOE spectroscopy (N0ESY)-heteronuclear multiple quantum correlation spectra and a 4-dimensional I3C/l3C-edited NOESY spectrum, along with 35 6, 9 xI , and 30 hydrogen bond constraints, were used to calculate 30 structures by a hybrid distance geometry/simulated annealing protocol, of which 24 were used for structural comparison. The calculations revealed that a 3-helix bundle packs against a small 4-stranded antiparallel P-sheet. The backbone RMS deviation (RMSD) for the family of structures was 1.03 * 0.19 A with respect to the average structure. The topology is analogous to that of the C-terminal domain of the catabolite gene activator protein and appears to be in the helix-turn-helix family of DNAbinding proteins. The overall fold determined by the NMR data is consistent with recent crystallographic work on this domain (Harrison CJ, Bohm AA, Nelson HCM, 1994, Science 263:224) as evidenced by RMSD between backbone atoms in the NMR and X-ray structures of 1.77 k 0.20 A. Several differences were identified some of which may be due to protein-protein interactions in the crystal.

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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).…”

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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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Heat shock factor is required for growth at normal temperatures in the fission yeast Schizosaccharomyces pombe.

Cited by 85 publications

References 49 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.

Solution structure of the DNA‐binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy

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

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