Activation by Heat Shock of hsp70 Gene Transcription in Sea Urchin Embryos

1995 ◽  
Vol 217 (3) ◽  
pp. 1032-1038 ◽  
Author(s):  
G. Sconzo ◽  
M.G. Ferraro ◽  
G. Amore ◽  
G. Giudice ◽  
D. Cascino ◽  
...  
Keyword(s):  
Heat Shock ◽  
Gene Transcription ◽  
Sea Urchin ◽  
Hsp70 Gene ◽  
Sea Urchin Embryos

Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells

1988 ◽  
Vol 8 (11) ◽  
pp. 4736-4744
Author(s):  
D D Mosser ◽  
N G Theodorakis ◽  
R I Morimoto
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Heat Shock ◽  
Gene Transcription ◽  
Elevated Temperatures ◽  
Binding Activity ◽  
Heat Shock Gene ◽  
Hsp70 Gene ◽  
Heat Shock Element ◽  
Amino Acid Analogs

Activation of human heat shock gene transcription by heat shock, heavy metal ions, and amino acid analogs required the heat shock element (HSE) in the HSP70 promoter. Both heat shock- and metal ion-induced HSP70 gene transcription occurred independently of protein synthesis, whereas induction by amino acid analogs required protein synthesis. We identified a HSE-binding activity from control cells which was easily distinguished by a gel mobility shift assay from the stress-induced HSE-binding activity which appeared following heat shock or chemically induced stress. The kinetics of HSP70 gene transcription paralleled the rapid appearance of stress-induced HSE-binding activity. During recovery from heat shock, both the rate of HSP70 gene transcription and stress-induced HSE-binding activity levels declined and the control HSE-binding activity reappeared. The DNA contacts of the control and stress-induced HSE-binding activities deduced by methylation interference were similar but not identical. While stable complexes with HSE were formed with extracts from both control and stressed cells in vitro at 25 degrees C, only the stress-induced complex was detected when binding reactions were performed at elevated temperatures.

Synthesis of ?heat shock? proteins in sea urchin embryos

1980 ◽  
Vol 4 (1) ◽  
pp. 69-74 ◽  
Author(s):  
G GIUDICE ◽  
M ROCCHERI ◽  
M DIBERNARDO
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Sea Urchin ◽  
Sea Urchin Embryos ◽  
Shock Proteins

Acquisition of thermotolerance in sea urchin embryos correlates with the synthesis and age of the heat shock proteins

1986 ◽  
Vol 19 (3) ◽  
pp. 173-177 ◽  
Author(s):  
G. Sconzo ◽  
M.C. Roccheri ◽  
M. La Rosa ◽  
D. Oliva ◽  
A. Abrignani ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Sea Urchin ◽  
Sea Urchin Embryos ◽  
Shock Proteins

Regulation of HSP70 by PTH: a model of gene regulation not mediated by changes in cAMP levels

1996 ◽  
Vol 271 (1) ◽  
pp. C121-C129 ◽  
Author(s):  
S. Fukayama ◽  
B. Lanske ◽  
J. Guo ◽  
H. M. Kronenberg ◽  
F. R. Bringhurst
Keyword(s):  
Heat Shock ◽  
Adenylate Cyclase ◽  
Gene Transcription ◽  
Cellular Response ◽  
Host Cells ◽  
Osteoblastic Cell ◽  
Target Cells ◽  
Hsp70 Gene ◽  
Hsp70 Mrna ◽  
Human Hsp70

Parathyroid hormone (PTH) activates both adenylate cyclase and phospholipase C in target cells, and cloned PTH/PTH-related protein (PTHrP) receptor can mediate both responses when expressed in host cells such as LLC-PK1 renal epithelial cells. Because calcitonin (CT) is known to augment 70-kDa heat shock protein (HSP70) mRNA by an adenosine 3',5'-cyclic monophosphate (cAMP)-independent mechanism in LLC-PK1 cells, we examined regulation of HSP70 transcription by PTH in these cells. Like CT, human PTH-(1-34) [hPTH-(1-34); 10(-10) to 10(-7) M)] increased porcine HSP70 mRNA and human HSP70 promoter-chloramphenicol acetyltransferase (CAT) expression within 4 h in LLC-PK1 cells that stably express > or = 100,000 PTH/PTHrP receptors per cell. The effect of PTH on HSP70 mRNA was not mimicked by cAMP analogues, forskolin, phorbol esters, Ca2+ ionophores, or alpha-thrombin; was insensitive to pertussis toxin; and was not due to increased mRNA stability. The upregulation of HSP70 gene transcription by hPTH (and CT) was clearly observed even after deletion of the functional heat shock consensus element in the promoter region of the human HSP70/CAT reporter. Upregulation of HSP70 transcription via endogenous PTH receptors also was observed in the osteoblastic cell lines SaOS-2 and ROS 17/2.8. Regulation of HSP70 gene transcription by PTH may be a common cellular response to the hormone, which, in some cells, may not be mediated by activation of adenylate cyclase or protein kinase C.

Expression and structural analysis of heat-shock genes in sea urchin embryos P. lividus

1989 ◽  
Vol 27 ◽  
pp. 19
Author(s):  
G. Sconzo ◽  
M. LaRosa ◽  
M.C. Roccheri ◽  
M.G. Ferraro ◽  
D. Buccheri ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Heat Shock ◽  
Sea Urchin ◽  
Heat Shock Genes ◽  
Sea Urchin Embryos

Turnover of histone acetyl groups during sea urchin early development is not required for histone, heat shock and actin gene transcription

1997 ◽  
Vol 1351 (1-2) ◽  
pp. 168-180 ◽  
Author(s):  
Algimantas Jasinskas ◽  
Dangeruta Kersulyte ◽  
John Langmore ◽  
Danguole Steponaviciute ◽  
Nijole Jasinskiene ◽  
...  
Keyword(s):  
Heat Shock ◽  
Early Development ◽  
Gene Transcription ◽  
Sea Urchin ◽  
Actin Gene

Gcn5- and Elp3-induced histone H3 acetylation regulates hsp70 gene transcription in yeast

2008 ◽  
Vol 409 (3) ◽  
pp. 779-788 ◽  
Author(s):  
Qiuju Han ◽  
Jun Lu ◽  
Jizhou Duan ◽  
Dongmei Su ◽  
Xiaozhe Hou ◽  
...  
Keyword(s):  
Heat Shock ◽  
Histone Acetylation ◽  
Rna Polymerase Ii ◽  
Gene Transcription ◽  
Transcriptional Activation ◽  
Histone H3 ◽  
Hsp70 Gene ◽  
Transcriptional Initiation ◽  
Hsp Genes ◽  
H3 Acetylation

The purpose of this study was to elucidate the mechanisms by which histone acetylation participates in transcriptional regulation of hsp70 (heat-shock protein 70) genes SSA3 and SSA4 in yeast. Our results indicated that histone acetylation was required for the transcriptional activation of SSA3 and SSA4. The HATs (histone acetyltransferases) Gcn5 (general control non-derepressible 5) and Elp3 (elongation protein 3) modulated hsp70 gene transcription by affecting the acetylation status of histone H3. Although the two HATs possessed overlapping function regarding the acetylation of histone H3, they affected hsp70 gene transcription in different ways. The recruitment of Gcn5 was Swi/Snf-dependent and was required for HSF (heat-shock factor) binding and affected RNAPII (RNA polymerase II) recruitment, whereas Elp3 exerted its roles mainly through affecting RNAPII elongation. These results provide insights into the effects of Gcn5 and Elp3 in hsp70 gene transcription and underscore the importance of histone acetylation for transcriptional initiation and elongation in hsp genes.

scholarly journals Inducible expression of a cloned heat shock fusion gene in sea urchin embryos.

1984 ◽  
Vol 81 (23) ◽  
pp. 7490-7494 ◽  
Author(s):  
A. P. McMahon ◽  
T. J. Novak ◽  
R. J. Britten ◽  
E. H. Davidson
Keyword(s):  
Heat Shock ◽  
Sea Urchin ◽  
Fusion Gene ◽  
Inducible Expression ◽  
Sea Urchin Embryos

scholarly journals Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells.

1988 ◽  
Vol 8 (11) ◽  
pp. 4736-4744 ◽  
Author(s):  
D D Mosser ◽  
N G Theodorakis ◽  
R I Morimoto
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Heat Shock ◽  
Gene Transcription ◽  
Elevated Temperatures ◽  
Binding Activity ◽  
Heat Shock Gene ◽  
Hsp70 Gene ◽  
Heat Shock Element ◽  
Amino Acid Analogs

Activation of human heat shock gene transcription by heat shock, heavy metal ions, and amino acid analogs required the heat shock element (HSE) in the HSP70 promoter. Both heat shock- and metal ion-induced HSP70 gene transcription occurred independently of protein synthesis, whereas induction by amino acid analogs required protein synthesis. We identified a HSE-binding activity from control cells which was easily distinguished by a gel mobility shift assay from the stress-induced HSE-binding activity which appeared following heat shock or chemically induced stress. The kinetics of HSP70 gene transcription paralleled the rapid appearance of stress-induced HSE-binding activity. During recovery from heat shock, both the rate of HSP70 gene transcription and stress-induced HSE-binding activity levels declined and the control HSE-binding activity reappeared. The DNA contacts of the control and stress-induced HSE-binding activities deduced by methylation interference were similar but not identical. While stable complexes with HSE were formed with extracts from both control and stressed cells in vitro at 25 degrees C, only the stress-induced complex was detected when binding reactions were performed at elevated temperatures.

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