The response of cells to a heat shock or other stresses is the activation of a small number of genes which were previously inactive or transcribed at low levels. This response has been observed in a wide variety of bacterial, plant, and animal species. Evidence is accumulating that at least some of the proteins found in diverse species are similar, indicating a conservation of the response and the proteins in evolution. In a number of organisms a strong positive correlation has been found between the presence of heat shock proteins and ability of the organism to withstand thermal stress. This review attempts to assess the available data concerning the homology of proteins in different species, the localization of the proteins in cells, and the relationship between heat shock proteins and thermoresistance.

The heat shock response.

A Drosophila RNA polymerase II transcription factor binds to the regulatory site of an hsp 70 gene.

The resistance to exonuclease digestion of two regions of chromatin at the 5′ end of heat-shock genes in Drosophila implies they have protein bound to them. The pattern of resistance before and after induction of gene expression suggests that heat-shock genes are activated by the sequential binding of at least two protein factors.

Two protein-binding sites in chromatin implicated in the activation of heat-shock genes.

Stress-induced transcriptional activation

New heat shock puffs and β=galactosidase activity resulting from transformation of Drosophila with an hsp70-lacZ hybrid gene

Heat-shock genes coding for heat-shock protein 70 (HSP70) in Drosophila melanogaster were subcloned into an SV40/plasmid recombinant capable of replication in permissive monkey COS cells. Following transfection of COS cells, no significant amount of Drosophila hsp70 RNA was detected at 37 degrees C. In contrast, a heat-shock at 43 degrees C or arsenite poisoning at 37 degrees C induced the massive production of Drosophila hsp70 RNA of correct size and faithful 5' ends. After heat-shock, the efficiency of hsp70 transcription in COS cells containing 2-4 X 10(4) gene copies was found to be 15-30% of that measured in Drosophila, on a per gene basis. By testing a series of 5' deletion mutants in this inducible transcription assay it was found that a sequence less than 70 bp long, directly upstream of the hsp70 gene, was essential for the heat or arsenite induction of transcription.

https://www.embopress.org/doi/pdf/10.1002/j.1460-2075.1982.tb00025.x

Regulation of heat-shock genes: a DNA sequence upstream of Drosophila hsp70 genes is essential for their induction in monkey cells.

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Regulation of heat-shock genes: a DNA sequence upstream of Drosophila hsp70 genes is essential for their induction in monkey cells.