Transient Expression of HSC70 in Cherry Fruit Subjected to Heat Shock (original) (raw)
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PLANT PHYSIOLOGY, 1996
prevented chilling injury from developing after 21 d at 2"C, whereas unheated fruit developed high levels of injury. Although the overall protein pattern as seen by Coomassie blue staining was similar from heated and unheated fruit, some high-and many low-molecularmass proteins were observed in the heated fruit that were absent or present in reduced amounts in unheated fruit. When fruit were injected with [35S]methionine at harvest and then heated, they accumulated high levels of specific radiolabeled proteins that could still be detected after 21 d at 2°C. If the fruit were held at 20°C after heating, the label in the proteins declined rapidly and these fruit were also sensitive to chilling injury. Hsp70 antibody reacted more strongly with proteins from heated and chilled fruit than with proteins from chilled fruit. Hspl8.1 antibody reacted strongly with proteins from heated fruit but not with those from unheated fruit. A 23-kD protein, highly labeled in heated fruit but not in unheated fruit, had its amino terminus sequenced. To our knowledge, this is the first report showing a relationship between the persistence of heat-shock proteins and chilling tolerance in a plant tissue.
International Journal of Fruit Science
Heat treatment has been shown to be an effective method for reducing systemic pathogens in strawberry but the process often has adverse effects on plant health. Research has shown that a brief heat treatment of plants at a lower temperature prior to the main heat treatment can induce heat shock proteins, which serve to protect the plant from damage when treated at higher temperatures. The objective of this study was to determine the relative gene expression of two heat shock factors (HSFs) and eight heat shock proteins (HSPs) in two strawberry cultivars (Festival and Ventana) known to have differential tolerance to heat. Strawberry plants were treated at 37°C for 1 hour to induce the heat shock response. Total RNA was extracted and reverse transcription polymerase chain reaction (RT-PCR) was used to determine the amount of target produced. Relative gene expression was determined using the 2 −ΔΔct method. Results showed that transcripts of one HSF and five HSPs were significantly more abundant in cv. Festival (p < 0.05) but transcripts from only one gene, sHsp15.96, were significantly more abundant in cv. Ventana. Results of this study have identified gene candidates that may confer heat tolerance in strawberry, which may be useful for selecting heat tolerant plants in breeding programs.
Journal of Food Biochemistry, 2010
Cherimoya is a major crop in the subtropical areas of the Spanish coast. The fruit are perishable because of their rapid climacteric ripening. Storage between 10 and 12C produces some extension of the shelf life of the fruit as a small delay in senescence is produced. A lower storage temperature produces chilling injury. The aim of this work is to find a way to make the fruit more resistant to low temperatures. In several plant species the synthesis of small molecular size heat-shock proteins (sHSPs) prevents and/or repairs stress induced damage; therefore, we investigated the induction of sHSPs in the mesocarp of cherimoya fruit. Heating the fruit at 55C during 5 h produces alleviation of the chilling-injury symptoms when the fruit are stored at 4C. The thermal stress induces proteins recognized by antibodies against sHSPs of different classes from other plant species. This induction is proportional to the temperature in the experimental range of 46-50C. PRACTICAL APPLICATIONS Refrigeration is the only described way to extent shelf life of cherimoya as senescence is delayed by the decreasing temperature. This is true until chilling injury appears. Senescence of this fruit occurs in 4-5 days when stored at 20C, which is a regular temperature in the production area. Storage at 10-12C allows commercialization during one additional week. Different attempts have been made to extend the period of conservation by using controlled atmosphere and lower temperatures. The problem is that cherimoya fruit are very susceptible to chilling injury. If a short heating treatment induces
Assessing `Bing' Sweet Cherry Tolerance to a Heated Controlled Atmosphere for Insect Pest Control
HortTechnology, 2001
Sweet cherries (Prunus avium `Bing') exposed to 113 or 117 °F (45 or 47 °C) in an atmosphere of 1% oxygen with 15% carbon dioxide (balance nitrogen) were heated to a maximum center temperature of 112 or 115 °F (44 or 46 °C) in 41 or 27 min, respectively. Heated cherries had similar incidence of pitting and decay, and similar preference ratings after 14 days of storage at 34 °F (1 °C) as nonheated or methyl bromide fumigated fruit. Heated cherries and methyl bromide fumigated cherries were less firm after 14 days of cold storage than nonheated, control fruit. The stems of methyl bromide fumigated cherries were less green than heated or nonheated cherries. Cherries exposed to 113 °F had lower titratable acidity than nonheated cherries, fumigated cherries, or cherries exposed to 117 °F. Cherry quality after 14 days of cold storage was not affected by hydrocooling before heating (5 min in water at 34 °F) or by method of cooling after heating (hydrocooling, forced air cooling, or sta...
Plant and Cell Physiology
The antibody prepared against one of the soybean (Glycine max) 15 to 18 kDa heat shock proteins (HSPs) that cross-reacted with the 12 polypeptides of 15 to 18 kDa class I low molecular weight (LMW) HSPs in soybean, was also found to cross-react in Western blot analyses with the class I LMW HSPs of nine other plant species, i.e., mung bean, pea, cucumber, tobacco, Arabidopsis, rice, maize, wheat, and barley. An antibody raised from the 16.9 kDa rice HSP also crossreacted with the same class I LMW HSPs of the ten plant species tested. HSPs-enriched fractions (70 to 100% ammonium sulfate saturation) prepared from mung bean and rice heat-shocked seedlings were able to thermostabilize the homologous soluble proteins, as we have shown previously in soybean. Up to 50% of the soluble proteins that are normally denatured by heating at 55°C for 30 min was protected when an HSPs-enriched fraction was added to either mung bean or rice protein. Additionally, the HSPs-enriched fractions were exchangeable among these three plant species for thermostabilization. The protection provided by these HSPs-enriched fractions is effective mainly for membrane-associated proteins. In soybean depletion of the 15 to 18 kDa HSPs in the HSPs-enriched fraction resulted in the loss of the thermostabilizing ability and when the 15 to 18 kDa HSPs were recovered in this fraction, the thermostabilizing ability was again restored. Thus, the 15 to 18 kDa HSPs in plant, which shuttle between the cytoplasm and cellular organelles during heat shock (HS) and recovery from HS, are responsible for providing the thermostabilization.
Plant and cell …, 1993
The antibody prepared against one of the soybean (Glycine max) 15 to 18 kDa heat shock proteins (HSPs) that cross-reacted with the 12 polypeptides of 15 to 18 kDa class I low molecular weight (LMW) HSPs in soybean, was also found to cross-react in Western blot analyses with the class I LMW HSPs of nine other plant species, i.e., mung bean, pea, cucumber, tobacco, Arabidopsis, rice, maize, wheat, and barley. An antibody raised from the 16.9 kDa rice HSP also crossreacted with the same class I LMW HSPs of the ten plant species tested. HSPs-enriched fractions (70 to 100% ammonium sulfate saturation) prepared from mung bean and rice heat-shocked seedlings were able to thermostabilize the homologous soluble proteins, as we have shown previously in soybean. Up to 50% of the soluble proteins that are normally denatured by heating at 55°C for 30 min was protected when an HSPs-enriched fraction was added to either mung bean or rice protein. Additionally, the HSPs-enriched fractions were exchangeable among these three plant species for thermostabilization. The protection provided by these HSPs-enriched fractions is effective mainly for membrane-associated proteins. In soybean depletion of the 15 to 18 kDa HSPs in the HSPs-enriched fraction resulted in the loss of the thermostabilizing ability and when the 15 to 18 kDa HSPs were recovered in this fraction, the thermostabilizing ability was again restored. Thus, the 15 to 18 kDa HSPs in plant, which shuttle between the cytoplasm and cellular organelles during heat shock (HS) and recovery from HS, are responsible for providing the thermostabilization.