scholarly journals In vivo transcriptional pausing and cap formation on three Drosophila heat shock genes.

1993 ◽  
Vol 90 (17) ◽  
pp. 7923-7927 ◽  
Author(s):  
E. B. Rasmussen ◽  
J. T. Lis
Keyword(s):  
Heat Shock ◽  
Heat Shock Genes ◽  
Transcriptional Pausing

scholarly journals The Skn7 Response Regulator ofSaccharomyces cerevisiaeInteracts with Hsf1 In Vivo and Is Required for the Induction of Heat Shock Genes by Oxidative Stress

2000 ◽  
Vol 11 (7) ◽  
pp. 2335-2347 ◽  
Author(s):  
Desmond C. Raitt ◽  
Anthony L. Johnson ◽  
Alexander M. Erkine ◽  
Kozo Makino ◽  
Brian Morgan ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Response Regulator ◽  
Coiled Coil ◽  
Normal Growth ◽  
Temperature Sensitive ◽  
Regulatory Sequences ◽  
Heat Shock Genes

The Skn7 response regulator has previously been shown to play a role in the induction of stress-responsive genes in yeast, e.g., in the induction of the thioredoxin gene in response to hydrogen peroxide. The yeast Heat Shock Factor, Hsf1, is central to the induction of another set of stress-inducible genes, namely the heat shock genes. These two regulatory trans-activators, Hsf1 and Skn7, share certain structural homologies, particularly in their DNA-binding domains and the presence of adjacent regions of coiled-coil structure, which are known to mediate protein–protein interactions. Here, we provide evidence that Hsf1 and Skn7 interact in vitro and in vivo and we show that Skn7 can bind to the same regulatory sequences as Hsf1, namely heat shock elements. Furthermore, we demonstrate that a strain deleted for the SKN7 gene and containing a temperature-sensitive mutation in Hsf1 is hypersensitive to oxidative stress. Our data suggest that Skn7 and Hsf1 cooperate to achieve maximal induction of heat shock genes in response specifically to oxidative stress. We further show that, like Hsf1, Skn7 can interact with itself and is localized to the nucleus under normal growth conditions as well as during oxidative stress.

scholarly journals A consensus sequence polymer inhibits in vivo expression of heat shock genes.

1986 ◽  
Vol 6 (9) ◽  
pp. 3200-3206 ◽  
Author(s):  
H Xiao ◽  
J T Lis
Keyword(s):  
Heat Shock ◽  
Consensus Sequence ◽  
Plasmid Vector ◽  
Regulatory Elements ◽  
Hsp70 Gene ◽  
Heat Shock Genes ◽  
Cis Acting ◽  
Consensus Sequences ◽  
Activity Measurements

Promoter function for hsp70 gene expression in Drosophila melanogaster was studied with an in vivo competition assay. A polymer of 40 tandem copies of the pair of regulatory elements of the hsp70 gene was constructed and cloned into a plasmid vector. Various marked genes were cotransfected with the polymer plasmid into Schneider line 2 cells, and their expression was determined by enzyme activity measurements. The polymer dramatically inhibited expression of cotransfected hsp70, hsp26, and hsp83 genes, but not cotransfected copia and histone genes. Our results indicate that in vivo, a trans-acting, positive regulatory factor, which can be titrated by heat shock consensus sequences, is required for activation of heat shock genes and is specific for these genes; the coordinate induction of different heat shock genes appears to be mediated by similar, but not identical, interactions of the trans-acting induction factor and the cis-acting heat shock consensus sequences; and the uninduced or basal level expression of the transfected hsp70 gene is also due to interaction of the consensus sequence with a positively acting factor.

scholarly journals Cdk7 Is Required for Full Activation of Drosophila Heat Shock Genes and RNA Polymerase II Phosphorylation In Vivo

2003 ◽  
Vol 23 (19) ◽  
pp. 6876-6886 ◽  
Author(s):  
Brian E. Schwartz ◽  
Stephane Larochelle ◽  
Beat Suter ◽  
John T. Lis
Keyword(s):  
Heat Shock ◽  
Rna Polymerase ◽  
Rna Polymerase Ii ◽  
Null Alleles ◽  
Temperature Sensitive ◽  
Heat Shock Genes ◽  
Elongation Complex ◽  
Pol Ii ◽  
Full Activation

ABSTRACT TFIIH has been implicated in several fundamental cellular processes, including DNA repair, cell cycle progression, and transcription. In transcription, the helicase activity of TFIIH functions to melt promoter DNA; however, the in vivo function of the Cdk7 kinase subunit of TFIIH, which has been hypothesized to be involved in RNA polymerase II (Pol II) phosphorylation, is not clearly understood. Using temperature-sensitive and null alleles of cdk7, we have examined the role of Cdk7 in the activation of Drosophila heat shock genes. Several in vivo approaches, including polytene chromosome immunofluorescence, nuclear run-on assays, and, in particular, a protein-DNA cross-linking assay customized for adults, revealed that Cdk7 kinase activity is required for full activation of heat shock genes, promoter-proximal Pol II pausing, and Pol II-dependent chromatin decondensation. The requirement for Cdk7 occurs very early in the transcription cycle. Furthermore, we provide evidence that TFIIH associates with the elongation complex much longer than previously suspected.

A consensus sequence polymer inhibits in vivo expression of heat shock genes

1986 ◽  
Vol 6 (9) ◽  
pp. 3200-3206
Author(s):  
H Xiao ◽  
J T Lis
Keyword(s):  
Heat Shock ◽  
Consensus Sequence ◽  
Plasmid Vector ◽  
Regulatory Elements ◽  
Hsp70 Gene ◽  
Heat Shock Genes ◽  
Cis Acting ◽  
Consensus Sequences ◽  
Activity Measurements

Promoter function for hsp70 gene expression in Drosophila melanogaster was studied with an in vivo competition assay. A polymer of 40 tandem copies of the pair of regulatory elements of the hsp70 gene was constructed and cloned into a plasmid vector. Various marked genes were cotransfected with the polymer plasmid into Schneider line 2 cells, and their expression was determined by enzyme activity measurements. The polymer dramatically inhibited expression of cotransfected hsp70, hsp26, and hsp83 genes, but not cotransfected copia and histone genes. Our results indicate that in vivo, a trans-acting, positive regulatory factor, which can be titrated by heat shock consensus sequences, is required for activation of heat shock genes and is specific for these genes; the coordinate induction of different heat shock genes appears to be mediated by similar, but not identical, interactions of the trans-acting induction factor and the cis-acting heat shock consensus sequences; and the uninduced or basal level expression of the transfected hsp70 gene is also due to interaction of the consensus sequence with a positively acting factor.

Reciprocal activation of HSF1 and HSF3 in brain and blood tissues: is redundancy developmentally related?

2006 ◽  
Vol 291 (3) ◽  
pp. R566-R572 ◽  
Author(s):  
Ariel Shabtay ◽  
Zeev Arad
Keyword(s):  
Heat Shock ◽  
Transcriptional Activity ◽  
Binding Activity ◽  
Cell Nuclei ◽  
Heat Shock Genes ◽  
Heat Shock Transcription Factors ◽  
Differentiated Cells ◽  
Dna Binding Activity ◽  
Response To Temperature

Transcriptional induction of heat-shock genes in response to temperature elevation and other stresses is mediated by heat-shock transcription factors (HSFs). Avian cells express two redundant heat-shock responsive factors, HSF1 and HSF3, which differ in their activation kinetics and threshold induction temperature. Unlike the ubiquitous activation of HSF1, the DNA-binding activity of HSF3 is restricted to undifferentiated avian cells and embryonic tissues. Herein, we report a reciprocal activation of HSF1 and HSF3 in vivo. Whereas HSF1 mediates transcriptional activity only in the brain upon severe heat shock, HSF3 is exclusively activated in blood cells upon light, moderate, and severe heat shock, promoting induction of heat-shock genes. Although not activated, HSF1 is expressed in blood cell nuclei in a granular appearance, suggesting regulation of genes other than heat-shock genes. Intraspecific comparison of heat-sensitive and heat-resistant fowl strains indicates that the unique activation pattern of HSF3 in blood tissue is a general phenomenon, not related to thermal history. Taken together, HSF1 and HSF3 mediate transcriptional activity of adult tissues and differentiated cells in a nonredundant manner. Instead, an exclusive, tissue-specific activation is observed, implying that redundancy may be developmentally related. The physiological and developmental implications are discussed.

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