Gene Bookmarking by the Heat-Shock Transcription Factor Programs the Insulin-Like Signaling Pathway

2021 ◽  
Author(s):  
Veena Prahlad ◽  
Srijit Das ◽  
Sehee Min
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Signaling Pathway ◽  
Heat Shock Transcription Factor ◽  
Gene Bookmarking

scholarly journals Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure.

1994 ◽  
Vol 14 (11) ◽  
pp. 7557-7568 ◽  
Author(s):  
J Zuo ◽  
R Baler ◽  
G Dahl ◽  
R Voellmy
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Heat Shock ◽  
Dna Binding ◽  
Hydrophobic Interactions ◽  
Coiled Coil ◽  
Heat Shock Transcription Factor ◽  
Single Amino Acid ◽  
Binding Ability ◽  
Heat Shock Element

Heat stress regulation of human heat shock genes is mediated by human heat shock transcription factor hHSF1, which contains three 4-3 hydrophobic repeats (LZ1 to LZ3). In unstressed human cells (37 degrees C), hHSF1 appears to be in an inactive, monomeric state that may be maintained through intramolecular interactions stabilized by transient interaction with hsp70. Heat stress (39 to 42 degrees C) disrupts these interactions, and hHSF1 homotrimerizes and acquires heat shock element DNA-binding ability. hHSF1 expressed in Xenopus oocytes also assumes a monomeric, non-DNA-binding state and is converted to a trimeric, DNA-binding form upon exposure of the oocytes to heat shock (35 to 37 degrees C in this organism). Because endogenous HSF DNA-binding activity is low and anti-hHSF1 antibody does not recognize Xenopus HSF, we employed this system for mapping regions in hHSF1 that are required for the maintenance of the monomeric state. The results of mutagenesis analyses strongly suggest that the inactive hHSF1 monomer is stabilized by hydrophobic interactions involving all three leucine zippers which may form a triple-stranded coiled coil. Trimerization may enable the DNA-binding function of hHSF1 by facilitating cooperative binding of monomeric DNA-binding domains to the heat shock element motif. This view is supported by observations that several different LexA DNA-binding domain-hHSF1 chimeras bind to a LexA-binding site in a heat-regulated fashion, that single amino acid replacements disrupting the integrity of hydrophobic repeats render these chimeras constitutively trimeric and DNA binding, and that LexA itself binds stably to DNA only as a dimer but not as a monomer in our assays.

Heat shock transcription factor 2 reduces the secretion of IL-1β by inhibiting NLRP3 inflammasome activation in ulcerative colitis

Gene ◽  
2021 ◽  
Vol 768 ◽  
pp. 145299
Author(s):  
Fengrui Zhang ◽  
Wei Zhao ◽  
Jiao Zhou ◽  
Wen Wang ◽  
Juan Luo ◽  
...  
Keyword(s):  
Ulcerative Colitis ◽  
Transcription Factor ◽  
Heat Shock ◽  
Nlrp3 Inflammasome ◽  
Heat Shock Transcription Factor ◽  
Inflammasome Activation ◽  
Nlrp3 Inflammasome Activation

Biochemical and Biophysical Characterization of the Trimerization Domain from the Heat Shock Transcription Factor†

Biochemistry ◽  
1999 ◽  
Vol 38 (12) ◽  
pp. 3559-3569 ◽  
Author(s):  
Ralph Peteranderl ◽  
Mark Rabenstein ◽  
Yeon-Kyun Shin ◽  
Corey W. Liu ◽  
David E. Wemmer ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Transcription Factor ◽  
Biophysical Characterization

Modulation of the Escherichia coli σ E (RpoE) heat‐shock transcription‐factor activity by the RseA, RseB and RseC proteins

1997 ◽  
Vol 24 (2) ◽  
pp. 355-371 ◽  
Author(s):  
Dominique Missiakas ◽  
Matthias P. Mayer ◽  
Marc Lemaire ◽  
Costa Georgopoulos ◽  
Satish Raina
Keyword(s):  
Escherichia Coli ◽  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Transcription Factor ◽  
Transcription Factor Activity ◽  
Factor Activity

Activation of the heat shock transcription factor by hypoxia in normal and tumor cell lines in vivo and in vitro

1992 ◽  
Vol 23 (4) ◽  
pp. 891-897 ◽  
Author(s):  
Amato J. Giaccia ◽  
Elizabeth A. Auger ◽  
Albert Koong ◽  
David J. Terris ◽  
Andrew I. Minchinton ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Tumor Cell ◽  
Cell Lines ◽  
Heat Shock Transcription Factor ◽  
Tumor Cell Lines

An alternatively spliced heat shock transcription factor,OsHSFA2dI, functions in the heat stress-induced unfolded protein response in rice

Plant Biology ◽  
2015 ◽  
Vol 17 (2) ◽  
pp. 419-429 ◽  
Author(s):  
Q. Cheng ◽  
Y. Zhou ◽  
Z. Liu ◽  
L. Zhang ◽  
G. Song ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Heat Stress ◽  
Heat Shock ◽  
Unfolded Protein Response ◽  
Heat Shock Transcription Factor ◽  
Unfolded Protein ◽  
Alternatively Spliced ◽  
Protein Response

miR-18, a member of Oncomir-1, targets heat shock transcription factor 2 in spermatogenesis

Development ◽  
2010 ◽  
Vol 137 (19) ◽  
pp. 3177-3184 ◽  
Author(s):  
J. K. Bjork ◽  
A. Sandqvist ◽  
A. N. Elsing ◽  
N. Kotaja ◽  
L. Sistonen
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Transcription Factor

scholarly journals Glycogen Synthase Kinase 3β and Extracellular Signal-Regulated Kinase Inactivate Heat Shock Transcription Factor 1 by Facilitating the Disappearance of Transcriptionally Active Granules after Heat Shock

1998 ◽  
Vol 18 (11) ◽  
pp. 6624-6633 ◽  
Author(s):  
Bin He ◽  
Yong-Hong Meng ◽  
Nahid F. Mivechi
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Transcriptional Activity ◽  
Glycogen Synthase ◽  
Heat Shock Transcription Factor ◽  
Glycogen Synthase Kinase 3Β ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Gsk 3Β ◽  
Transcription Factor 1

ABSTRACT Heat shock transcription factor 1 (HSF-1) activates the transcription of heat shock genes in eukaryotes. Under normal physiological growth conditions, HSF-1 is a monomer. Its transcriptional activity is repressed by constitutive phosphorylation. Upon activation, HSF-1 forms trimers, acquires DNA binding activity, increases transcriptional activity, and appears as punctate granules in the nucleus. In this study, using bromouridine incorporation and confocal laser microscopy, we demonstrated that newly synthesized pre-mRNAs colocalize to the HSF-1 punctate granules after heat shock, suggesting that these granules are sites of transcription. We further present evidence that glycogen synthase kinase 3β (GSK-3β) and extracellular signal-regulated kinase mitogen-activated protein kinase (ERK MAPK) participate in the down regulation of HSF-1 transcriptional activity. Transient increases in the expression of GSK-3β facilitate the disappearance of HSF-1 punctate granules and reduce hsp-70 transcription after heat shock. We have also shown that ERK is the priming kinase for GSK-3β. Taken together, these results indicate that GSK-3β and ERK MAPK facilitate the inactivation of activated HSF-1 after heat shock by dispersing HSF-1 from the sites of transcription.

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