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.

The sensitivity of in situ hybridization has been increased at least 10-fold by hybridizing in cDNA excess, by increasing the diffusion of the cDNA through the cells, by hybridizing at optimum temperature, and by stabilizing hybrids during autoradiography. Saturation of intracellular RNA with [3H]cDNA has been achieved. The assay is quantitative. In situ hybridization has been used to detect and quantitate visna virus RNA in infected cells. By using [3H]cDNA with specific activity of 2 X 10(8) dpm/micrograms and conditions that reduce background to negligible levels, 10--20 copies of viral RNA per cell can be detected and quantitated after 2 days of autoradiographic exposure.

Detection of viral sequences of low reiteration frequency by in situ hybridization

The induction of heat-shock transcription factor (HSF) binding to DNA is accomplished by a heat-induced oligomerization. The transition to the induced state is accompanied by a chromosomal redistribution of HSF to the heat-shock puff sites. Over 150 additional chromosomal sites also accumulate HSF, including developmental loci that are repressed during heat shock. These findings suggest an unforeseen role for HSF as a represser of normal gene activity during heat stress.

Stress-induced oligomerization and chromosomal relocalization of heat-shock factor.

Attempts to investigate the cellular localization of keratin mRNAs byin situ hybridization with specific [35S]-labelled cDNA probes to mouse epithelia have been seriously impeded by the uncontrollable detachment of frozen tissue sections on conventionally coated glass slides (i.e. those coated with egg white, gelatine, collagen). Similarly, a variety of other coating and attachment devices have proved to be unsatisfactory or impracticable for large scale investigations. These difficulties were completely overcome andin situ hybridization was possible after a short immersion of the glass slides in a 2% solution of 3-aminopropyltriethoxysilane in acetone. This treatment provides the glass surface with aminoalkyl groups which are apparently able to react covalently with aldehyde or ketone functions of frozen tissue sections. The resulting firm adhesion of the sections enabled us to investigate the influence of different fixation and prehybridization procedures on the quality of thein situ hybridization. It was found that especially harsh prehybridization, involving hydrochloric acid, heat and proteinase K treatment, drastically reduces the morphological integrity of the sections, thus rendering a reliable assignment of the label difficult. In contrast, a mild prehybridization, consisting mainly of a rehydration of the sections in phosphate-buffered saline and equilibration in 0.1 M glycine, leaves the morphology intact and leads to a highly efficient and specificin situ hybridization.

Aminoalkylsilane-treated glass slides as support for in situ hybridization of keratin cDNAs to frozen tissue sections under varying fixation and pretreatment conditions.

Varying patterns of protein synthesis in Drosophila during heat shock: Implications for regulation

Cytoplasmic RNA from imaginal discs of Drosophila melanogaster, labeled by uridine incorporation in organ culture, has been assayed by hybridization to cytological preparations of polytene chromosomes. RNA labeled during the early stages (first four hours) of ecdysone stimulation was compared to RNA labeled in the absence of the hormone. For the poly(A)-containing fraction (oligo-dT bound), several loci hybridize only RNA labeled in the presence of ecdysone; one locus hybridizes only control RNA. The majority of hybridizing loci are unaffected by the hormone. Of the loci hybridizing RNA not bound to oligo-dT, several appear specific for the ecdysone-treated sample, though most are labeled more heavily with this RNA than with the control. None of the ecdysone-sensitive loci visualized by in situ hybridization are the sites of salivary gland puffs induced by ecdysone on the same time scale.

Ecdysone-stimulated RNA synthesis in imaginal discs of Drosophila melanogaster. Assay by in situ hybridization.

The effect of heat shock on RNA synthesis in Drosophila tissues.

https://www.cell.com/cell/pdf/0092-8674(77)90199-4.pdf

Ecdysone-stimulated RNA synthesis in salivary glands of drosophila melanogaster: assay by in situ hybridization.

Polytene chromosome puffing and in situ hybridization measure different aspects of RNA metabolism.

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Ecdysone-stimulated RNA synthesis in imaginal discs of Drosophila melanogaster. Assay by in situ hybridization.

The effect of heat shock on RNA synthesis in Drosophila tissues.

Ecdysone-stimulated RNA synthesis in salivary glands of drosophila melanogaster: assay by in situ hybridization.

Polytene chromosome puffing and in situ hybridization measure different aspects of RNA metabolism.