Structure of human heat-shock transcription factor 1 in complex with DNA

2016 ◽  
Vol 23 (2) ◽  
pp. 140-146 ◽  
Author(s):  
Tobias Neudegger ◽  
Jacob Verghese ◽  
Manajit Hayer-Hartl ◽  
F Ulrich Hartl ◽  
Andreas Bracher
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Transcription Factor ◽  
Transcription Factor 1

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 Homology Modeling and Characterization of Novel Stress Inducing Genes and their Split Sites Recognition in the Genome of Zebra Fish (Danio Rario) by Employing Special Consensus Pattern Matching Algorithms- using an in-Silico Method.

2019 ◽  
Vol 9 (1) ◽  
pp. 6715-6720
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Pattern Matching ◽  
Binding Sites ◽  
In Silico ◽  
3D Structure ◽  
Transcription Factor Binding Sites ◽  
Heat Shock Transcription Factor ◽  
Zebra Fish ◽  
Transcription Factor 1

Zebra fish has long been considered to be as a strong animal model in biology and modern genetics; however now a days its gaining lot of importance in environmental studies as well. The readily availability of entire genome sequences made to permit carrying out in silico studies at Genomic level. As everyone is known that stress is much more complex and complicated process that involves so much of gene regulations known as up regulation and down regulation, the corresponding stress proteins, broadly known as heat shock proteins. In the current study, the potential transcription factor binding sites were traced out by using bioinformatics tools and about 50 heat shock protein genes were predicted by using special alogorithms using pattern matching and position weight matrices. The 3D structure of DNA-binding domain of HSTF-1 ( Heat Shock Transcription factor-1) which is crucial for regulating heat shot proteins was traced out and builted by using homology modelling methods. The 3D structure of the heat shock transcription factor-1 and together with predicted transcription factor binding sites may be validated in future experimental works which would help us in understanding the complex responsive stress mechanisms lying in Zebra fish.

scholarly journals Heat Shock Transcription Factor 1 Is Involved in Quality-Control Mechanisms in Male Germ Cells1

2004 ◽  
Vol 70 (1) ◽  
pp. 18-24 ◽  
Author(s):  
Hanae Izu ◽  
Sachiye Inouye ◽  
Mitsuaki Fujimoto ◽  
Koji Shiraishi ◽  
Katsusuke Naito ◽  
...  
Keyword(s):  
Quality Control ◽  
Transcription Factor ◽  
Heat Shock ◽  
Heat Shock Transcription Factor ◽  
Control Mechanisms ◽  
Transcription Factor 1

Absence of heat shock transcription factor 1 retards the regrowth of atrophied soleus muscle in mice

2011 ◽  
Vol 111 (4) ◽  
pp. 1142-1149 ◽  
Author(s):  
Kazuyuki Yasuhara ◽  
Yoshitaka Ohno ◽  
Atsushi Kojima ◽  
Kenji Uehara ◽  
Moroe Beppu ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Stress Response ◽  
Heat Shock ◽  
Soleus Muscle ◽  
Heat Shock Transcription Factor ◽  
Hindlimb Suspension ◽  
Wild Type ◽  
Muscle Weight ◽  
Cross Sectional ◽  
Transcription Factor 1

Effects of heat shock transcription factor 1 (HSF1) gene on the regrowth of atrophied mouse soleus muscles were studied. Both HSF1-null and wild-type mice were subjected to continuous hindlimb suspension for 2 wk followed by 4 wk of ambulation recovery. There was no difference in the magnitude of suspension-related decrease of muscle weight, protein content, and the cross-sectional area of muscle fibers between both types of mice. However, the regrowth of atrophied soleus muscle in HSF1-null mice was slower compared with that in wild-type mice. Lower baseline expression level of HSP25, HSC70, and HSP72 were noted in soleus muscle of HSF1-null mice. Unloading-associated downregulation and reloading-associated upregulation of HSP25 and HSP72 mRNA were observed not only in wild-type mice but also in HSF1-null mice. Reloading-associated upregulation of HSP72 and HSP25 during the regrowth of atrophied muscle was observed in wild-type mice. Minor and delayed upregulation of HSP72 at mRNA and protein levels was also seen in HSF1-null mice. Significant upregulations of HSF2 and HSF4 were observed immediately after the suspension in HSF1-null mice, but not in wild-type mice. Therefore, HSP72 expression in soleus muscle might be regulated by the posttranscriptional level, but not by the stress response. Evidence from this study suggested that the upregulation of HSPs induced by HSF1-associated stress response might play, in part, important roles in the mechanical loading (stress)-associated regrowth of skeletal muscle.

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