Transcripts from the Drosophila heat-shock gene hsr-omega influence rates of protein synthesis but hardly affect resistance to heat knockdown

2011 ◽  
Vol 285 (4) ◽  
pp. 313-323 ◽  
Author(s):  
Travis K. Johnson ◽  
Fiona E. Cockerell ◽  
Stephen W. McKechnie
1992 ◽  
Vol 117 (6) ◽  
pp. 1151-1159 ◽  
Author(s):  
R Baler ◽  
WJ Welch ◽  
R Voellmy

Heat shock genes encode proteins (hsp's) that play important structural roles under normal circumstances and are essential to the cells' ability to survive environmental insults. Evidence is presented herein that transcriptional regulation of hsp gene expression is linked with the regulation of overall protein synthesis as well as with the accumulation of proteins denatured by stressful events. The factor that connects the three processes appears to be one of the hsp's, presumably a member(s) of the hsp70 family. Biochemical experiments demonstrate that complexes containing hsp70 and heat shock transcription factor, the specific regulator of hsp gene activity, are formed in the cells.


1988 ◽  
Vol 263 (24) ◽  
pp. 11718-11728 ◽  
Author(s):  
D T Chin ◽  
S A Goff ◽  
T Webster ◽  
T Smith ◽  
A L Goldberg

1988 ◽  
Vol 8 (11) ◽  
pp. 4736-4744
Author(s):  
D D Mosser ◽  
N G Theodorakis ◽  
R I Morimoto

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.


2018 ◽  
Vol 506 (4) ◽  
pp. 799-804 ◽  
Author(s):  
Ryan Oliverio ◽  
Peter Nguyen ◽  
Brianna Kdeiss ◽  
Sara Ord ◽  
Amanda J. Daniels ◽  
...  

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