Regulation of gene expression in corn (<i>Zea mays</i> L.) by heat shock

Baszczynski, Chris L.; Walden, D. B.; Atkinson, Burr G.

doi:10.1139/o82-070

Cited by 83 publications

(43 citation statements)

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“…In contrast, Baszczynski et al (1), in studies on the effects of heat shock on corn roots and shoots, showed no changes between the complements of in vivo labeled proteins from intact and excised tissues as visualized by one-dimensional gel electrophoresis and fluorography.…”

Section: And Discussionmentioning

confidence: 87%

Ribonucleic Acid and Protein Metabolism in Pea Epicotyls

Schuster

Davies²

1983

Plant Physiol.

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Aged pea Pisum sativum L. var Alaska epicotyl tissue was wounded by excising the apical 10 or 20 millimeters and incubating the excised segments upright in buffer. Wounding induced a very rapid formation of polysomes which was accompanied by minor increases in ribosomes, mRNA, and poly(A) and by a doubling of the in vivo protein synthesizing capacity. This increase in protein synthesis in vivo was matched by a similar increase in polypeptide synthesis in vitro in wheat germ reactions primed by polysomes. However, in vitro reactions primed by total and polysomal RNA from wounded tissue were affected much less.Two-dimensional gel patterns of silver-stained proteins accumulated in vivo were almost unchanged, even after 6 hours of wounding, since only two spots decreased in intensity and none increased. In contrast, two-dimensional gel fluorographs of polypeptides generated in vitro by both total RNA and polysomal RNA showed numerous changes within 3 hours of wounding. Of the more than 200 spots visualized by fluorography, 17 decreased and 26 increased when total RNA from wounded tissue was used; 15 decreased and 10 increased when polysomal RNA was used. Those polypeptides that decreased after wounding were generally of lower molecular weight; those which increased were of higher molecular weight.Although wounding must be affecting transcription insofar as different mRNAs must be present to encode different polypeptides, its major effect appears to be on translation, presumably through formation of ribosomes with greater translational efficiency.

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Section: And Discussionmentioning

confidence: 87%

Ribonucleic Acid and Protein Metabolism in Pea Epicotyls

Schuster

Davies²

1983

Plant Physiol.

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“…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).…”

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confidence: 91%

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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“…This protein whose synthesis is enhanced in heat shocked mitochondria does not correspond to any of the HSPs induced by temperature or other stress in corn (2,5). It is possible that the concentration of this 52 kD protein is so small in total seedlings that it would be undetectable in total protein extracts.…”

Section: Discussionmentioning

confidence: 96%

“…The role of this protein in the heat shock response is discussed in light of the implication of mitochondria as the primary cellular target to temperature stress. Higher plants, including corn, respond rapidly to an upward shift in incubation temperature by synthesizing a set of HSPs3 (2,5,9). Thermotolerance is the proposed function of the HSPs.…”

Section: S-methionine Incorporationmentioning

confidence: 99%