scholarly journals B-Myb and cyclin D1 mediate heat shock element dependent activation of the human HSP70 promoter

Oncogene ◽  
1997 ◽  
Vol 14 (10) ◽  
pp. 1223-1229 ◽  
Author(s):  
Hiroshi Kamano ◽  
Karl-Heinz Klempnauer
Keyword(s):  
Heat Shock ◽  
Cyclin D1 ◽  
Hsp70 Promoter ◽  
Heat Shock Element ◽  
Human Hsp70

TATA-dependent and TATA-independent function of the basal and heat shock elements of a human hsp70 promoter

1990 ◽  
Vol 10 (4) ◽  
pp. 1319-1328
Author(s):  
J M Greene ◽  
R E Kingston
Keyword(s):  
Heat Shock ◽  
Consensus Sequence ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Hsp70 Promoter ◽  
Heat Shock Element ◽  
Tata Element ◽  
Sequence Elements ◽  
Human Heat Shock Protein ◽  
Human Hsp70

We have characterized the interactions between the TATA element and other sequence elements of a human heat shock protein 70 (hsp70) promoter by a mutational approach. Expression of a distal element of this promoter requires an intact TATA element in human cell lines. The hsp70 TATA element can be functionally replaced for this interaction by TATA elements from the simian virus 40 early and adenovirus EIIa promoters. The TATA element in this promoter therefore both determines the appropriate start site and determines strength by allowing function of the distal element. In contrast, three proximal upstream elements necessary for basal and heat-regulated transcription have no requirement either for a TATA element or for any other proximal element. The behavior of promoters multiply mutant in these proximal elements implies that these elements function independently. We examined the interaction between the heat shock element (HSE) and the TATA element as the distance between the two factor-binding sites was increased. It was necessary to create a mutant HSE with an extended consensus sequence in order for the HSE to function at a distance. Moving this extended HSE 500 bases upstream did not increase its dependence on the TATA element, suggesting that the TATA independence of this element is intrinsic to its function and is not determined by distance from the promoter.

Heat shock-induced interactions of heat shock transcription factor and the human hsp70 promoter examined by in vivo footprinting

1991 ◽  
Vol 11 (1) ◽  
pp. 586-592
Author(s):  
K Abravaya ◽  
B Phillips ◽  
R I Morimoto
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Consensus Sequence ◽  
Regulatory Elements ◽  
Heat Shock Transcription Factor ◽  
Hsp70 Promoter ◽  
Heat Shock Element ◽  
In Vivo Footprinting ◽  
Human Hsp70

Genomic footprinting of the human hsp70 promoter reveals that heat shock induces a rapid binding of a factor, presumably heat shock transcription factor, to a region encompassing five contiguous NGAAN sequences, three perfect and two imperfect matches to the consensus sequence. Arrays of inverted NGAAN sequences have been defined as the heat shock element. No protein is bound to the heat shock element prior to or after recovery from heat shock. Heat shock does not perturb the binding of factors to other regulatory elements in the promoter which contribute to basal expression of the hsp70 gene.

scholarly journals TATA-dependent and TATA-independent function of the basal and heat shock elements of a human hsp70 promoter.

1990 ◽  
Vol 10 (4) ◽  
pp. 1319-1328 ◽  
Author(s):  
J M Greene ◽  
R E Kingston
Keyword(s):  
Heat Shock ◽  
Consensus Sequence ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Hsp70 Promoter ◽  
Heat Shock Element ◽  
Tata Element ◽  
Sequence Elements ◽  
Human Heat Shock Protein ◽  
Human Hsp70

We have characterized the interactions between the TATA element and other sequence elements of a human heat shock protein 70 (hsp70) promoter by a mutational approach. Expression of a distal element of this promoter requires an intact TATA element in human cell lines. The hsp70 TATA element can be functionally replaced for this interaction by TATA elements from the simian virus 40 early and adenovirus EIIa promoters. The TATA element in this promoter therefore both determines the appropriate start site and determines strength by allowing function of the distal element. In contrast, three proximal upstream elements necessary for basal and heat-regulated transcription have no requirement either for a TATA element or for any other proximal element. The behavior of promoters multiply mutant in these proximal elements implies that these elements function independently. We examined the interaction between the heat shock element (HSE) and the TATA element as the distance between the two factor-binding sites was increased. It was necessary to create a mutant HSE with an extended consensus sequence in order for the HSE to function at a distance. Moving this extended HSE 500 bases upstream did not increase its dependence on the TATA element, suggesting that the TATA independence of this element is intrinsic to its function and is not determined by distance from the promoter.

Heat-inducible human factor that binds to a human hsp70 promoter

1987 ◽  
Vol 7 (4) ◽  
pp. 1530-1534
Author(s):  
R E Kingston ◽  
T J Schuetz ◽  
Z Larin
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein 70 ◽  
Human Factor ◽  
Regulatory Factor ◽  
Hsp70 Promoter ◽  
Heat Shock Element ◽  
Initial Event ◽  
Nuclear Extracts ◽  
Human Heat Shock Protein ◽  
Human Hsp70

A factor found in nuclear extracts of human cells bound to the heat shock element of a human heat shock protein 70 gene. The level of this factor was significantly increased after heat shock. This induction was rapid and was not blocked by cycloheximide, suggesting that an initial event in the response of a human cell to heat is the activation of a preexisting regulatory factor.

scholarly journals Heat shock-induced interactions of heat shock transcription factor and the human hsp70 promoter examined by in vivo footprinting.

1991 ◽  
Vol 11 (1) ◽  
pp. 586-592 ◽  
Author(s):  
K Abravaya ◽  
B Phillips ◽  
R I Morimoto
Keyword(s):  
Transcription Factor ◽  
Heat Shock ◽  
Consensus Sequence ◽  
Regulatory Elements ◽  
Heat Shock Transcription Factor ◽  
Hsp70 Promoter ◽  
Heat Shock Element ◽  
In Vivo Footprinting ◽  
Human Hsp70

Genomic footprinting of the human hsp70 promoter reveals that heat shock induces a rapid binding of a factor, presumably heat shock transcription factor, to a region encompassing five contiguous NGAAN sequences, three perfect and two imperfect matches to the consensus sequence. Arrays of inverted NGAAN sequences have been defined as the heat shock element. No protein is bound to the heat shock element prior to or after recovery from heat shock. Heat shock does not perturb the binding of factors to other regulatory elements in the promoter which contribute to basal expression of the hsp70 gene.

scholarly journals Heat-inducible human factor that binds to a human hsp70 promoter.

1987 ◽  
Vol 7 (4) ◽  
pp. 1530-1534 ◽  
Author(s):  
R E Kingston ◽  
T J Schuetz ◽  
Z Larin
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein 70 ◽  
Human Factor ◽  
Regulatory Factor ◽  
Hsp70 Promoter ◽  
Heat Shock Element ◽  
Initial Event ◽  
Nuclear Extracts ◽  
Human Heat Shock Protein ◽  
Human Hsp70

A factor found in nuclear extracts of human cells bound to the heat shock element of a human heat shock protein 70 gene. The level of this factor was significantly increased after heat shock. This induction was rapid and was not blocked by cycloheximide, suggesting that an initial event in the response of a human cell to heat is the activation of a preexisting regulatory factor.

scholarly journals Mouse heat shock transcription factors 1 and 2 prefer a trimeric binding site but interact differently with the HSP70 heat shock element.

1993 ◽  
Vol 13 (6) ◽  
pp. 3370-3383 ◽  
Author(s):  
P E Kroeger ◽  
K D Sarge ◽  
R I Morimoto
Keyword(s):  
Transcription Factors ◽  
Heat Shock ◽  
Binding Site ◽  
Heat Shock Element ◽  
Heat Shock Transcription Factors ◽  
Adjacent Site ◽  
Differential Binding ◽  
Dyad Symmetry ◽  
Human Hsp70

To understand the function of multiple heat shock transcription factors in higher eukaryotes, we have characterized the interaction of recombinant mouse heat shock transcription factors 1 and 2 (mHSF1 and mHSF2) with their binding site, the heat shock element (HSE). For our analysis, we utilized the human HSP70 HSE, which consists of three perfect 5'-nGAAn-3' sites (1, 3, and 4) and two imperfect sites (2 and 5) arranged as tandem inverted repeats. Recombinant mHSF1 and mHSF2, which exist as trimers in solution, both bound specifically to this HSE and stimulated transcription of a human HSP70-CAT construct in vitro. Footprinting analyses revealed differential binding of mHSF1 and mHSF2 to the HSP70 HSE. Specifically, mHSF1 bound all five pentameric sites, whereas mHSF2 failed to interact with the first site of the HSE but bound to sites 2 to 5. Missing-nucleoside analysis demonstrated that the third and fourth nGAAn sites were essential for mHSF1 and mHSF2 binding. The binding of the initial mHSF1 trimer to the HSE exhibited preference for sites 3, 4, and 5, and then binding of a second trimer occurred at sites 1 and 2. These results suggest that HSF may recognize its binding site through the dyad symmetry of sites 3 and 4 but requires an adjacent site for stable interaction. Our data demonstrate that mHSF1 and mHSF2 bind specifically to the HSE through major groove interactions. Methidiumpropyl-EDTA footprinting revealed structural differences in the first and third repeats of the HSE, suggesting that the DNA is distorted in this region. The possibility that the HSE region is naturally distorted may assist in understanding how a trimer of HSF can bind to what is essentially an inverted repeat binding site.

scholarly journals Maximal stress-induced transcription from the human HSP70 promoter requires interactions with the basal promoter elements independent of rotational alignment.

1990 ◽  
Vol 10 (6) ◽  
pp. 3125-3136 ◽  
Author(s):  
G T Williams ◽  
R I Morimoto
Keyword(s):  
Heat Shock ◽  
Physiological Stress ◽  
Inducible Promoter ◽  
Inducible Expression ◽  
Promoter Elements ◽  
Transient Transfection Assay ◽  
Heat Shock Element ◽  
Cis Acting ◽  
Maximal Stress ◽  
Human Hsp70

Transcription of the human HSP70 gene is regulated by a complex array of cis-acting promoter elements that respond to conditions that include normal conditions of cell growth and induction following physiological stress. We have examined the requirements of the basal and inducible promoter elements by using promoter mutations and a transient transfection assay. Multiple forms of stress-induced transcription, including heat shock and incubation with heavy metals or amino acid analogs, are mediated by a single heat shock element (HSE) between -105 and -91 consisting of three contiguous 5-base-pair units, NGAAN, that are inverted relative to adjacent units. Maximal inducible expression requires a fully functional basal promoter. Spacing mutations which alter the relative helical orientation of adjacent genetic elements have only minimal effects on basal and stress-inducible expression and show no effects of periodicity. In addition, placement of the HSE adjacent to the basal promoter removes the requirements for a fully functional basal promoter for maximal stress-inducible expression. These results suggest that factors bound at the HSE and the basal promoter can function through multiple interactions.

Mouse heat shock transcription factors 1 and 2 prefer a trimeric binding site but interact differently with the HSP70 heat shock element

1993 ◽  
Vol 13 (6) ◽  
pp. 3370-3383
Author(s):  
P E Kroeger ◽  
K D Sarge ◽  
R I Morimoto
Keyword(s):  
Transcription Factors ◽  
Heat Shock ◽  
Binding Site ◽  
Heat Shock Element ◽  
Heat Shock Transcription Factors ◽  
Adjacent Site ◽  
Differential Binding ◽  
Dyad Symmetry ◽  
Human Hsp70

To understand the function of multiple heat shock transcription factors in higher eukaryotes, we have characterized the interaction of recombinant mouse heat shock transcription factors 1 and 2 (mHSF1 and mHSF2) with their binding site, the heat shock element (HSE). For our analysis, we utilized the human HSP70 HSE, which consists of three perfect 5'-nGAAn-3' sites (1, 3, and 4) and two imperfect sites (2 and 5) arranged as tandem inverted repeats. Recombinant mHSF1 and mHSF2, which exist as trimers in solution, both bound specifically to this HSE and stimulated transcription of a human HSP70-CAT construct in vitro. Footprinting analyses revealed differential binding of mHSF1 and mHSF2 to the HSP70 HSE. Specifically, mHSF1 bound all five pentameric sites, whereas mHSF2 failed to interact with the first site of the HSE but bound to sites 2 to 5. Missing-nucleoside analysis demonstrated that the third and fourth nGAAn sites were essential for mHSF1 and mHSF2 binding. The binding of the initial mHSF1 trimer to the HSE exhibited preference for sites 3, 4, and 5, and then binding of a second trimer occurred at sites 1 and 2. These results suggest that HSF may recognize its binding site through the dyad symmetry of sites 3 and 4 but requires an adjacent site for stable interaction. Our data demonstrate that mHSF1 and mHSF2 bind specifically to the HSE through major groove interactions. Methidiumpropyl-EDTA footprinting revealed structural differences in the first and third repeats of the HSE, suggesting that the DNA is distorted in this region. The possibility that the HSE region is naturally distorted may assist in understanding how a trimer of HSF can bind to what is essentially an inverted repeat binding site.

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