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 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

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.

scholarly journals An internal region of the RpoH heat shock transcription factor is critical for rapid degradation by the FtsH protease

FEBS Letters ◽  
2001 ◽  
Vol 493 (1) ◽  
pp. 17-20 ◽  
Author(s):  
Dino Bertani ◽  
Amos B. Oppenheim ◽  
Franz Narberhaus
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Transcription Factor ◽  
Rapid Degradation ◽  
Internal Region ◽  
Ftsh Protease

Role of heat shock transcription factor in yeast metallothionein gene expression

1991 ◽  
Vol 11 (7) ◽  
pp. 3676-3681
Author(s):  
W M Yang ◽  
W Gahl ◽  
D Hamer
Keyword(s):  
Gene Expression ◽  
Transcription Factor ◽  
Heat Shock ◽  
Gene Transcription ◽  
Heat Shock Factor ◽  
Heat Shock Transcription Factor ◽  
Wild Type ◽  
Promoter Sequences ◽  
Metallothionein Gene ◽  
Upstream Promoter

The induction of Saccharomyces cerevisiae metallothionein gene transcription by Cu and Ag is mediated by the ACE1 transcription factor. In an effort to detect additional stimuli and factors that regulate metallothionein gene transcription, we isolated a Cu-resistant suppressor mutant of an ACE1 deletion strain. Even in the absence of metals, the suppressor mutant exhibited high basal levels of metallothionein gene transcription that required upstream promoter sequences. The suppressor gene was cloned, and its predicted product was shown to correspond to yeast heat shock transcription factor with a single-amino-acid substitution in the DNA-binding domain. The mutant heat shock factor bound strongly to metallothionein gene upstream promoter sequences, whereas wild-type heat shock factor interacted weakly with the same region. Heat treatment led to a slight but reproducible induction of metallothionein gene expression in both wild-type and suppressor strains, and Cd induced transcription in the mutant strain. These studies provide evidence for multiple pathways of metallothionein gene transcriptional regulation in S. cerevisiae.

Modular recognition of 5-base-pair DNA sequence motifs by human heat shock transcription factor

1991 ◽  
Vol 11 (7) ◽  
pp. 3504-3514
Author(s):  
N F Cunniff ◽  
J Wagner ◽  
W D Morgan
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Gene Promoter ◽  
Heat Shock Transcription Factor ◽  
Heat Shock Gene ◽  
Gene Promoters ◽  
Sequence Motifs ◽  
Binding Modes ◽  
Heat Shock Element

We investigated the recognition of the conserved 5-bp repeated motif NGAAN, which occurs in heat shock gene promoters of Drosophila melanogaster and other eukaryotic organisms, by human heat shock transcription factor (HSF). Extended heat shock element mutants of the human HSP70 gene promoter, containing additional NGAAN blocks flanking the original element, showed significantly higher affinity than the wild-type promoter element for human HSF in vitro. Protein-DNA contact positions were identified by hydroxyl radical protection, diethyl pyrocarbonate interference, and DNase I footprinting. New contacts in the mutant HSE constructs corresponded to the locations of additional NGAAN motifs. The pattern of binding indicated the occurrence of multiple DNA binding modes for HSF with the various constructs and was consistent with an oligomeric, possibly trimeric, structure of the protein. In contrast to the improved binding, the extended heat shock element mutant constructs did not exhibit dramatically increased heat-inducible transcription in transient expression assays with HeLa cells.

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