Temperature-dependent increase in the DNA-binding activity of a heat shock factor in an extract of tobacco cultured cells

1996 ◽  
Vol 31 (1) ◽  
pp. 13-22 ◽  
Author(s):  
Sae Shimizu ◽  
Yoshinobu Itoh ◽  
Ken-ichi Yamazaki
Keyword(s):  
Heat Shock ◽  
Dna Binding ◽  
Cultured Cells ◽  
Heat Shock Factor ◽  
Binding Activity ◽  
Temperature Dependent ◽  
Dna Binding Activity

scholarly journals Azadiradione ameliorates polyglutamine expansion disease in Drosophila by potentiating DNA binding activity of heat shock factor 1

Oncotarget ◽  
2016 ◽  
Vol 7 (48) ◽  
pp. 78281-78296 ◽  
Author(s):  
Vinod K. Nelson ◽  
Asif Ali ◽  
Naibedya Dutta ◽  
Suvranil Ghosh ◽  
Manas Jana ◽  
...  
Keyword(s):  
Heat Shock ◽  
Dna Binding ◽  
Heat Shock Factor ◽  
Binding Activity ◽  
Heat Shock Factor 1 ◽  
Polyglutamine Expansion ◽  
Dna Binding Activity

scholarly journals Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress.

1993 ◽  
Vol 13 (3) ◽  
pp. 1392-1407 ◽  
Author(s):  
K D Sarge ◽  
S P Murphy ◽  
R I Morimoto
Keyword(s):  
Heat Shock ◽  
Dna Binding ◽  
Gene Transcription ◽  
Nuclear Localization ◽  
Heat Shock Factor ◽  
Binding Activity ◽  
Heat Shock Gene ◽  
Dna Binding Activity ◽  
Shock Gene ◽  
In Cells

The existence of multiple heat shock factor (HSF) genes in higher eukaryotes has promoted questions regarding the functions of these HSF family members, especially with respect to the stress response. To address these questions, we have used polyclonal antisera raised against mouse HSF1 and HSF2 to examine the biochemical, physical, and functional properties of these two factors in unstressed and heat-shocked mouse and human cells. We have identified HSF1 as the mediator of stress-induced heat shock gene transcription. HSF1 displays stress-induced DNA-binding activity, oligomerization, and nuclear localization, while HSF2 does not. Also, HSF1 undergoes phosphorylation in cells exposed to heat or cadmium sulfate but not in cells treated with the amino acid analog L-azetidine-2-carboxylic acid, indicating that phosphorylation of HSF1 is not essential for its activation. Interestingly, HSF1 and HSF2 overexpressed in transfected 3T3 cells both display constitutive DNA-binding activity, oligomerization, and transcriptional activity. These results demonstrate that HSF1 can be activated in the absence of physiological stress and also provide support for a model of regulation of HSF1 and HSF2 activity by a titratable negative regulatory factor.

Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress

1993 ◽  
Vol 13 (3) ◽  
pp. 1392-1407
Author(s):  
K D Sarge ◽  
S P Murphy ◽  
R I Morimoto
Keyword(s):  
Heat Shock ◽  
Dna Binding ◽  
Gene Transcription ◽  
Nuclear Localization ◽  
Heat Shock Factor ◽  
Binding Activity ◽  
Heat Shock Gene ◽  
Dna Binding Activity ◽  
Shock Gene ◽  
In Cells

The existence of multiple heat shock factor (HSF) genes in higher eukaryotes has promoted questions regarding the functions of these HSF family members, especially with respect to the stress response. To address these questions, we have used polyclonal antisera raised against mouse HSF1 and HSF2 to examine the biochemical, physical, and functional properties of these two factors in unstressed and heat-shocked mouse and human cells. We have identified HSF1 as the mediator of stress-induced heat shock gene transcription. HSF1 displays stress-induced DNA-binding activity, oligomerization, and nuclear localization, while HSF2 does not. Also, HSF1 undergoes phosphorylation in cells exposed to heat or cadmium sulfate but not in cells treated with the amino acid analog L-azetidine-2-carboxylic acid, indicating that phosphorylation of HSF1 is not essential for its activation. Interestingly, HSF1 and HSF2 overexpressed in transfected 3T3 cells both display constitutive DNA-binding activity, oligomerization, and transcriptional activity. These results demonstrate that HSF1 can be activated in the absence of physiological stress and also provide support for a model of regulation of HSF1 and HSF2 activity by a titratable negative regulatory factor.

scholarly journals Molecular Basis for SUMOylation-dependent Regulation of DNA Binding Activity of Heat Shock Factor 2

2008 ◽  
Vol 284 (4) ◽  
pp. 2435-2447 ◽  
Author(s):  
Yukihiro Tateishi ◽  
Mariko Ariyoshi ◽  
Ryuji Igarashi ◽  
Hideyuki Hara ◽  
Kenji Mizuguchi ◽  
...  
Keyword(s):  
Heat Shock ◽  
Dna Binding ◽  
Molecular Basis ◽  
Heat Shock Factor ◽  
Binding Activity ◽  
Dna Binding Activity

Interaction between heat shock factor and hsp70 is insufficient to suppress induction of DNA-binding activity in vivo

1994 ◽  
Vol 14 (10) ◽  
pp. 6552-6560
Author(s):  
S K Rabindran ◽  
J Wisniewski ◽  
L Li ◽  
G C Li ◽  
C Wu
Keyword(s):  
Heat Shock ◽  
Dna Binding ◽  
Heat Shock Proteins ◽  
Expression System ◽  
Stress Protein ◽  
Binding Activity ◽  
Protein Family ◽  
Oligomeric State ◽  
Dna Binding Activity ◽  
Shock Proteins

The intracellular level of free heat shock proteins, in particular the 70-kDa stress protein family, has been suggested to be the basis of an autoregulatory mechanism by which the cell measures the level of thermal stress and regulates the synthesis of heat shock proteins. It has been proposed that the DNA-binding and oligomeric state of the heat shock transcription factor (HSF) is a principal step in the induction pathway that is responsive to the level of 70-kDa stress protein. To test this hypothesis, we investigated the association between HSF and 70-kDa stress protein by means of a coimmunoprecipitation assay. We found that 70-kDa stress proteins associate to similar extents with both latent and active forms of HSF, although unlike other 70-kDa stress protein substrates, the association with HSF was not significantly disrupted in the presence of ATP. Gel mobility shift assays indicated that active HSF trimers purified from a bacterial expression system could not be substantially deactivated in vitro with purified 70-kDa stress protein and ATP. In addition, elevated concentrations of hsp70 alone could not significantly inhibit induction of the DNA-binding activity of endogenous HSF in cultured rat cells, and the induction was also not inhibited in cultured rat cells or Drosophila cells containing elevated levels of all members of the heat shock protein family. However, the deactivation of HSF to the non-DNA-binding state after prolonged heat stress or during recovery could be accelerated by increased levels of heat shock proteins. Hence, the level of heat shock proteins may affect the rate of disassembly of HSF trimers, but another mechanism, as yet undefined, appears to control the onset of the oligomeric transitions.

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