The Expression of Heat Shock Genes — A Model for Environmental Stress Response

Schöffl, Fritz; Baumann, Götz; Raschke, Eberhard

doi:10.1007/978-3-7091-6950-6_14

Cited by 17 publications

(11 citation statements)

References 78 publications

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“…The mature pollen is a specialized haploid tissue, that contains a store of presynthesized mRNA used for pollen germination and tube growth (18). The synthesis of HSPs is primarily regulated by a transcriptional control, allowing rapid induction of mRNA and a preferential translation during heat shock (24). Pollen is dormant in its mature state and is a gametophytic tissue which has a restricted developmental program.…”

Section: Discussionmentioning

confidence: 99%

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Influence of Temperature Stress on in Vitro Fertilization and Heat Shock Protein Synthesis in Maize (Zea mays L.) Reproductive Tissues

Dupuis¹,

Dumas²

1990

Plant Physiol.

211

122

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This study was conducted to investigate the response of maize (Zea mays) male and female mature reproductive tissues to temperature stress. We have tested the fertilization abilities of the stressed spikelets and pollen using in vitro pollination-fertilization to determine their respective tolerance to stress. The synthesis of heat shock proteins (HSPs) was also analyzed in male and female tissues using electrophoresis of 35S-labeled proteins and fluorography, to establish a relationship between the physiological and molecular responses. Pollen, spikelets, and pollinated spikelets were exposed to selected temperatures (4, 28, 32, 36, or 400C) and tested using an in vitro fertilization system. The fertilization rate is highly reduced when pollinated spikelets are exposed to temperatures over 360C. When pollen and spikelets are exposed separately to temperature stress, the female tissues appear resistant to 4 hours of cold stress (40C) or heat stress (40°C). Under heat shock conditions, the synthesis of a typical set of HSPs is induced in the female tissues. In contrast, the mature pollen is sensitive to heat stress and is responsible for the failure of fertilization at high temperatures. At the molecular level, no heat shock response is detected in the mature pollen.

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Section: Discussionmentioning

confidence: 99%

“…When plants and animals (6) are subjected to elevated temperatures, they respond by synthesizing a specific set of proteins, the HSPs3 (24). This heat shock response has been observed in a wide variety of vegetative tissues in maize, including plumules (1), roots (4), coleoptiles, scutellum, leaves, and cultured cells (5).…”

mentioning

confidence: 99%

Influence of Temperature Stress on in Vitro Fertilization and Heat Shock Protein Synthesis in Maize (Zea mays L.) Reproductive Tissues

Dupuis¹,

Dumas²

1990

Plant Physiol.

211

122

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“…5) are associated with the MT/PM fraction of the density gradient (12). There have been several reports of the localization of low molecular weight HSPs in mitochondria and plastids of plant cells (23). In heat-shocked soybean seedlings proteins with Mr between 20,000 and 25,000 become associated with both mitochondria (17) and plastids (25).…”

Section: Discussionmentioning

confidence: 99%

Heat Shock Inhibits α-Amylase Synthesis in Barley Aleurone without Inhibiting the Activity of Endoplasmic Reticulum Marker Enzymes

Sticher

Biswas²,

Bush³

et al. 1990

Plant Physiol.

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The effects of heat shock on the synthesis of a-amylase and on the membranes of the endoplasmic reticulum (ER) of barley (Hordeum vulgare) aleurone were studied. Heat shock, imposed by raising the temperature of incubation from 250C to 400C for 3 hours, inhibits the accumulation of a-amylase and other proteins in the incubation medium of barley aleurone layers treated with gibberellic acid and Ca2 . When ER is isolated from heat-shocked aleurone layers, less newly synthesized a-amylase is found associated with this membrane system. ER membranes, as indicated by the activities of NADH cytochrome c reductase and ATPdependent Ca2+ transport, are not destroyed by heat stress, however. Although heat shock did not reduce the activity of ER membrane marker enzymes, it altered the buoyant density of these membranes. Whereas ER from control tissue showed a peak of marker enzyme activity at 27% to 28% sucrose (1.113-1.120 grams per cubic centimeter), ER from heat-shocked tissue peaked at 30% to 32% sucrose (1.127-1.137 grams per cubic centimeter). The synthesis of a group of proteins designated as heat-shock proteins (HSPs) was stimulated by heat shock. These HSPs were localized to different compartments of the aleurone cell. Several proteins ranging from 15 to 30 kilodaltons were found in the ER and the mitochondrial/plasma membrane fractions of heat-shocked cells, but none of the HSPs accumulated in the incubation medium of heat-shocked aleurone layers.

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“…It represents a palindromic element with repetitive purine and pyrimidine motifs: 5'-nGAAnnTTCnnGAAnnTTCn-3' (Amin et al, 1988;Nover, 1987;Schoffl et al, 1988;Xiao and Lis, 1988). Different methods have been used for the characterization and purification of the postulated heat stress transcription factor (HSF) from Drosophila (Topol et al, 1985;Wiederrecht et al, 1988;Wu et al, 1987), yeast Pelham, 1987, 1988;Wiederrecht et al, 1988) and mammals (Goldenberg et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

Three tomato genes code for heat stress transcription factors with a region of remarkable homology to the DNA-binding domain of the yeast HSF.

et al. 1990

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The Expression of Heat Shock Genes — A Model for Environmental Stress Response

Cited by 17 publications

References 78 publications

Influence of Temperature Stress on in Vitro Fertilization and Heat Shock Protein Synthesis in Maize (Zea mays L.) Reproductive Tissues

Influence of Temperature Stress on in Vitro Fertilization and Heat Shock Protein Synthesis in Maize (Zea mays L.) Reproductive Tissues

Heat Shock Inhibits α-Amylase Synthesis in Barley Aleurone without Inhibiting the Activity of Endoplasmic Reticulum Marker Enzymes

Three tomato genes code for heat stress transcription factors with a region of remarkable homology to the DNA-binding domain of the yeast HSF.

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