The yeast heat shock transcription factor contains a transcriptional activation domain whose activity is repressed under nonshock conditions

Nieto-Sotelo, J.; Wiederrecht, Gregory; Okuda, Akihiko; Parker, Carl S.

doi:10.1016/0092-8674(90)90124-w

Cited by 165 publications

(166 citation statements)

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“…Activation-induced oligomerization of HSF1 is controlled by intra-and intermolecular hydrophobic interactions mediated by several conserved repeated motifs. [35][36][37] Deletion of certain conserved regions of HSF1 leads to its constitutive trimerization and activation (reviewed in Voellmy 38 ).…”

Section: Introductionmentioning

confidence: 99%

Spermatocyte-specific expression of constitutively active heat shock factor 1 induces HSP70i-resistant apoptosis in male germ cells

et al. 2005

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Spermatocytes, the most sensitive male germ cells to heatinduced apoptosis, do not respond to hyperthermia by inducing heat shock proteins (HSPs), including HSP70i, which has been previously shown to confer resistance to apoptosis in somatic cells. To dissect the mechanism of heat-induced apoptosis and to determine if we could protect spermatocytes by expressing HSP70i, we engineered transgenic mice that express in spermatocytes constitutively active heat shock transcription factor (HSF)1. Such HSF1 expression did not lead to transcription of inducible Hsp70 genes, but instead induced caspase-dependent apoptosis that mimicked heat shock-induced death of spermatogenic cells. Both mitochondria-dependent and death receptor-dependent pathways appear to be involved in such HSF1-induced apoptosis: the levels of Bcl-2 family proteins became increased, p53 protein accumulated and expression levels of caspase-8 and deathreceptor-interacting proteins (including Fas-associated death domain protein and TNF receptor associated death domain protein) became elevated. Surprisingly, the constitutive spermatocyte-specific expression of HSP70i in doubletransgenic males did not protect against such HSF1-induced apoptosis.

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Section: Introductionmentioning

confidence: 99%

Spermatocyte-specific expression of constitutively active heat shock factor 1 induces HSP70i-resistant apoptosis in male germ cells

et al. 2005

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“…HSF is bound constitutively to the heat shock promoter element (HSE) at all temperatures in the yeast Saccharomyces cerevisiae, and its transcriptional activity is correlated with changes in phosphorylation (22,36,49,50). In higher eukaryotes HSF activation involves conversion of the inactive factor to a form that is capable of specifically binding to the HSE (25,48,61).…”

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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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“…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). The DNA-binding activity directs HSF to heat shock elements, defined as a series of inverted repeats of the 5-base pair sequence nGAAn (Amin et al, 1988;Xiao & Lis, 1988;Perisic et al, 1989;Boorstein & Craig, 1990;Xiao et al, 1991).…”

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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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The yeast heat shock transcription factor contains a transcriptional activation domain whose activity is repressed under nonshock conditions

Cited by 165 publications

References 40 publications

Spermatocyte-specific expression of constitutively active heat shock factor 1 induces HSP70i-resistant apoptosis in male germ cells

Spermatocyte-specific expression of constitutively active heat shock factor 1 induces HSP70i-resistant apoptosis in male germ cells

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

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