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 (6) ◽  
pp. 3838-3839 ◽  
Keyword(s):  
Heat Shock ◽  
Dna Binding ◽  
Gene Transcription ◽  
Nuclear Localization ◽  
Heat Shock Factor ◽  
Binding Activity ◽  
Heat Shock Gene ◽  
Heat Shock Factor 1 ◽  
Dna Binding Activity ◽  
Shock Gene

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 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 AIRAP, a New Human Heat Shock Gene Regulated by Heat Shock Factor 1

2010 ◽  
Vol 285 (18) ◽  
pp. 13607-13615 ◽  
Author(s):  
Antonio Rossi ◽  
Edoardo Trotta ◽  
Rossella Brandi ◽  
Ivan Arisi ◽  
Marta Coccia ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Factor ◽  
Heat Shock Gene ◽  
Heat Shock Factor 1 ◽  
Shock Gene

Human heat shock factors 1 and 2 are differentially activated and can synergistically induce hsp70 gene transcription

1994 ◽  
Vol 14 (3) ◽  
pp. 2087-2099
Author(s):  
L Sistonen ◽  
K D Sarge ◽  
R I Morimoto
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Dna Binding ◽  
Gene Transcription ◽  
K562 Cells ◽  
Heat Shock Gene ◽  
Hsp70 Gene ◽  
Heat Shock Factors ◽  
Shock Gene ◽  
Heat Shock Gene Expression

Two members of the heat shock transcription factor (HSF) family, HSF1 and HSF2, both function as transcriptional activators of heat shock gene expression. However, the inducible DNA-binding activities of these two factors are regulated by distinct pathways. HSF1 is activated by heat shock and other forms of stress, whereas HSF2 is activated during hemin-induced differentiation of human K562 erythroleukemia cells, suggesting a role for HSF2 in regulating heat shock gene expression under nonstress conditions such as differentiation and development. To understand the distinct regulatory pathways controlling HSF2 and HSF1 activities, we have examined the biochemical and physical properties of the control and activated states of HSF2 and compared these with the properties of HSF1. Our results reveal that the inactive, non-DNA-binding forms of HSF2 and HSF1 exist primarily in the cytoplasm of untreated K562 cells as a dimer and monomer, respectively. This difference in the control oligomeric states suggests that the mechanisms used to control the DNA-binding activities of HSF2 and HSF1 are distinct. Upon activation, both factors acquire DNA-binding activity, oligomerize to a trimeric state, and translocate into the nucleus. Interestingly, we find that simultaneous activation of both HSF2 and HSF1 in K562 cells subjected to hemin treatment followed by heat shock results in the synergistic induction of hsp70 gene transcription, suggesting a novel level of complex regulation of heat shock gene expression.

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