Structures of Heat Shock Factor Trimers Bound to DNA Reveal the Panoramic Architecture of the HSF-Regulated Transcriptional Machinery

2021 ◽  
Author(s):  
Na Feng ◽  
Han Feng ◽  
Sheng Wang ◽  
Avinash S. Punekar ◽  
Rudolf Ladenstein ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Factor ◽  
Transcriptional Machinery

A Novel Triazole Nucleoside Suppresses Prostate Cancer Cell Growth by Inhibiting Heat Shock Factor 1 and Androgen Receptor

2015 ◽  
Vol 15 (10) ◽  
pp. 1333-1340 ◽  
Author(s):  
Yi Xia ◽  
Menghua Wang ◽  
Eliana Beraldi ◽  
Mei Cong ◽  
Amina Zoubeidi ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Androgen Receptor ◽  
Heat Shock ◽  
Cell Growth ◽  
Cancer Cell ◽  
Prostate Cancer Cell ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Cancer Cell Growth

scholarly journals The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress.

1996 ◽  
Vol 16 (3) ◽  
pp. 839-846 ◽  
Author(s):  
E M Newton ◽  
U Knauf ◽  
M Green ◽  
R E Kingston
Keyword(s):  
Amino Acids ◽  
Heat Shock ◽  
Transcriptional Activation ◽  
Heat Shock Factor ◽  
Acid Activation ◽  
Regulatory Domain ◽  
Activation Domain ◽  
Control Temperature ◽  
Activation Domains ◽  
Transcriptional Activation Domains

Heat shock factor (HSF) activates transcription in response to cellular stress. Human HSF1 has a central regulatory domain which can repress the activity of its activation domains at the control temperature and render them heat shock inducible. To determine whether the regulatory domain works in tandem with specific features of the HSF1 transcriptional activation domains, we first used deletion and point mutagenesis to define these activation domains. One of the activation domains can be reduced to just 20 amino acids. A GAL4 fusion protein containing the HSF 1 regulatory domain and this 20-amino-acid activation domain is repressed at the control temperature but potently activates transcription in response to heat shock. No specific amino acids in this activation domain are required for response to the regulatory domain; in particular, none of the potentially phosphorylated serine and threonine residues are required for heat induction, implying that heat-induced phosphorylation of the transcriptional activation domains is not required for induction. The regulatory domain is able to confer heat responsiveness to an otherwise completely heterologous chimeric activator that contains a portion of the VP16 activation domain, suggesting that the regulatory domain can sense heat in the absence of other portions of HSF1.

scholarly journals Effects of neurohormonal stress and aging on the activation of mammalian heat shock factor 1.

1994 ◽  
Vol 269 (51) ◽  
pp. 32272-32278
Author(s):  
T W Fawcett ◽  
S L Sylvester ◽  
K D Sarge ◽  
R I Morimoto ◽  
N J Holbrook
Keyword(s):  
Heat Shock ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1
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