scholarly journals A heat shock element in the phosphoglycerate kinase gene promoter of yeast

1988 ◽  
Vol 16 (4) ◽  
pp. 1333-1348 ◽  
Author(s):  
P.W. Piper ◽  
B. Curran ◽  
M.W. Davies ◽  
K. Hirst ◽  
A. Lockheart ◽  
...  
Keyword(s):  
Heat Shock ◽  
Phosphoglycerate Kinase ◽  
Gene Promoter ◽  
Heat Shock Element ◽  
Kinase Gene ◽  
Phosphoglycerate Kinase Gene

Stimulation of Yeast 3-Phosphoglycerate Kinase Gene Promoter by Paraquat

2000 ◽  
Vol 270 (3) ◽  
pp. 1036-1040 ◽  
Author(s):  
Neville Vassallo ◽  
Dolores R. Galea ◽  
William H. Bannister ◽  
Rena Balzan
Keyword(s):  
Phosphoglycerate Kinase ◽  
Gene Promoter ◽  
Kinase Gene ◽  
Phosphoglycerate Kinase Gene ◽  
Stimulation Of

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.

scholarly journals Expression of a constitutively active mutant of heat shock factor 1 under the control of testis-specific hst70 gene promoter in transgenic mice induces degeneration of seminiferous epithelium.

2003 ◽  
Vol 50 (2) ◽  
pp. 535-541 ◽  
Author(s):  
Wiesława Widłak ◽  
Konrad Benedyk ◽  
Natallia Vydra ◽  
Magdalena Głowala ◽  
Dorota Scieglińska ◽  
...  
Keyword(s):  
Heat Shock ◽  
Transgenic Mice ◽  
Target Genes ◽  
Gene Promoter ◽  
Basic Mechanism ◽  
Seminiferous Epithelium ◽  
High Rate ◽  
Heat Shock Factor 1 ◽  
Heat Shock Element ◽  
Constitutively Active

Heat shock activates in somatic cells a set of genes encoding heat shock proteins which function as molecular chaperones. The basic mechanism by which these genes are activated is the interaction of the specific transcription factor HSF1 with a regulatory DNA sequence called heat shock element (HSE). In higher eukaryotes HSF1 is present in unstressed cells as inactive monomers which, in response to cellular stress, aggregate into transcriptionally competent homotrimers. In the present paper we showed that the expression of a transgene encoding mutated constitutively active HSF1 placed under the control of a spermatocyte-specific promoter derived from the hst70 gene severely affects spermatogenesis. We found the testes of transgenic mice to be significantly smaller than those of wild-type males and histological analysis showed massive degeneration of the seminiferous epithelium. The lumen of tubules was devoid of spermatids and spermatozoa and using the TUNEL method we demonstrated a high rate of spermatocyte apoptosis. The molecular mechanism by which constitutively active HSF1 arrests spermatogenesis is not known so far. One can assume that HSF1 can either induce or repress so far unknown target genes involved in germ cell apoptosis.

Demethylation of specific sites in the 5' region of the inactive X-linked human phosphoglycerate kinase gene correlates with the appearance of nuclease sensitivity and gene expression

1988 ◽  
Vol 8 (11) ◽  
pp. 4692-4699
Author(s):  
R S Hansen ◽  
N A Ellis ◽  
S M Gartler
Keyword(s):  
Cell Lines ◽  
X Chromosome ◽  
Transcriptional Activation ◽  
Hybrid Cell ◽  
Methylation Status ◽  
Phosphoglycerate Kinase ◽  
Kinase Gene ◽  
Inactive X Chromosome ◽  
Phosphoglycerate Kinase Gene ◽  
Hypoxanthine Guanine Phosphoribosyltransferase

X8/6T2, a hamster-human hybrid cell line which contains an inactive human X chromosome, was treated with 5-azacytidine and selected for derepression of hypoxanthine-guanine phosphoribosyltransferase. Clones were examined for coreactivation of the phosphoglycerate kinase gene (Pgk). Of 68 of these hybrids, approximately 20% expressed measurable human phosphoglycerate kinase (PGK) activity. A 600-base-pair region of the Pgk 5' CpG cluster was examined for the methylation status of eight CCGG sites (site 1 being 5'-most) in a number of PGK-negative and PGK-positive cell lines. The inactive X chromosome is normally methylated at all eight sites, and this was also true for the majority of X8/6T2 cells. However, several PGK-negative hybrids were demethylated in the site 3 to site 6 region. PGK activity correlated with demethylation at both sites 6 and 7. The data for PGK-positive and -negative hybrids indicate that demethylation at or near site 7 was necessary for reactivation of Pgk. Chromatin sensitivity to MspI digestion in the nuclei of male lymphoblastoid cells and several PGK-positive and PGK-negative hybrids was examined. PGK-positive cell lines were hypersensitive to digestion, while PGK-negative hybrids were resistant. Cleavage at sites 6 and 7 was observed in all PGK-positive cell lines at each MspI concentration examined. Sites 7 and 8 were less accessible to digestion than site 6. Cleavage in the site 2 to site 5 region was observable at the lowest MspI concentration. In most PGK-positive hybrids, a nonspecific endogenous nuclease detected the presence of a hypersensitive region spanning at least 450 base pairs, bounded at the 3' end near HpaII site 6. Nuclease hypersensitivity appears to be related to promoter activity, because sites 7 and 8 are in transcribed regions of the gene. These data indicate that specific sites within the CpG cluster have a dominant controlling influence over the Pgk promoter conformation and the transcriptional activation of Pgk.

scholarly journals Nucleotide Sequence of a Wheat Chloroplastic Phosphoglycerate Kinase Gene

1995 ◽  
Vol 107 (4) ◽  
pp. 1483-1484 ◽  
Author(s):  
P. G. Jones ◽  
C. A. Raines ◽  
J. C. Lloyd
Keyword(s):  
Nucleotide Sequence ◽  
Phosphoglycerate Kinase ◽  
Kinase Gene ◽  
Phosphoglycerate Kinase Gene

scholarly journals Regulation of human heme oxygenase-1 gene expression under thermal stress

Blood ◽  
1996 ◽  
Vol 87 (12) ◽  
pp. 5074-5084 ◽  
Author(s):  
S Okinaga ◽  
K Takahashi ◽  
K Takeda ◽  
M Yoshizawa ◽  
H Fujita ◽  
...  
Keyword(s):  
Gene Expression ◽  
Thermal Stress ◽  
Heat Shock ◽  
Transient Expression ◽  
Reporter Gene ◽  
Heme Oxygenase ◽  
Gene Promoter ◽  
Heme Oxygenase 1 ◽  
Heat Shock Element ◽  
Hsp70 Mrna

Heme oxygenase-1 is an essential enzyme in heme catabolism, and its human gene promoter contains a putative heat shock element (HHO-HSE). This study was designed to analyze the regulation of human heme oxygenase-1 gene expression under thermal stress. The amounts of heme oxygenase-1 protein were not increased by heat shock (incubation at 42 degrees C) in human alveolar macrophages and in a human erythroblastic cell line, YN-1–0-A, whereas heat shock protein 70 (HSP70) was noticeably induced. However, heat shock factor does bind in vitro to HHO-HSE and the synthetic HHO-HSE by itself is sufficient to confer the increase in the transient expression of a reporter gene upon heat shock. The deletion of the sequence, located downstream from HHO-HSE, resulted in the activation of a reporter gene by heat shock. These results suggest that HHO-HSE is potentially functional but is repressed in vivo. Interestingly, heat shock abolished the remarkable increase in the levels of heme oxygenase-1 mRNA in YN-1–0-A cells treated with hemin or cadmium, in which HSP70 mRNA was noticeably induced. Furthermore, transient expression assays showed that heat shock inhibits the cadmium-mediated activation of the heme oxygenase-1 promoter, whereas the HSP70 gene promoter was activated upon heat shock. Such regulation of heme oxygenase-1 under thermal stress may be of physiologic significance in erythroid cells.

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