Immunological kinship of class I low molecular weight heat shock proteins and thermostabilization of soluble proteins in vitro among plants (original) (raw)
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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 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 exch...
Plant physiology, 1997
A monospecific polyclonal antibody was used to study the tissue-type specificity and intracellular localization of class I low-molecular-weight (LMW) heat-shock proteins (HSPs) in soybean (Glycine max) under different heat-shock regimes. In etiolated soybean seedlings, the root meristematic regions contained the highest levels of LMW HSP. No tissue-type-specific expression of class I LMW HSP was detected using the tissue-printing method. In immunolocalization studies of seedlings treated with HS (40[deg]C for 2 h) the class I LMW HSPs were found in the aggregated granular structures, which were distributed randomly in the cytoplasm and in the nucleus. When the heat shock was released, the granular structures disappeared and the class I LMW HSPs became distributed homogeneously in the cytoplasm. When the seedlings were then given a more severe heat shock following the initial 40[deg]C -> 28[deg]C treatment, a large proportion of the class I LMW HSPs that originally localized in th...
A Class of Soybean Low Molecular Weight Heat Shock Proteins : Immunological Study and Quantitation
PLANT PHYSIOLOGY, 1992
Two major polypeptides of the 15-to 18-kilodalton class of soybean (Glycine max) heat shock proteins (HSPs), obtained from an HSP-enriched (NH4)2SO4 fraction separated by two-dimensional polyacrylamide gel electrophoresis, were used individually as antigens to prepare antibodies. Each of these antibody preparations reacted with its antigen and cross-reacted with 12 other 15-to 18kilodalton HSPs. With these antibodies, the accumulation of the 15-to 18-kilodalton HSPs under various heat shock (HS) conditions was quantified. The 15-to 18-kilodalton HSPs began to be detectable at 350C, and after 4 hours at 40'C they had accumulated to a maximum level of 1.54 micrograms per 100 micrograms of total protein in soybean seedlings and remained almost unchanged up to 24 hours after HS. Accumulation of the HSPs was reduced at temperatures higher than 400C. At 42.50C the HSPs were reduced to 1.02 micrograms per 100 micrograms, and at 450C they were hardly detectable. A brief HS at 45'C (10 minutes), followed by incubation at 280C, which also induced HSP synthesis, resulted in synthesis of this class of HSPs at levels up to 1.06 micrograms per 100 micrograms of total protein. Taking into consideration the previous data concerning the acquisition of thermotolerance in soybean seedlings, our estimation indicates that the accumulation of the 15to 18-kilodalton HSPs to 0.76 to 0.98% of total protein correlated well with the establishment of thermotolerance. Of course, other HSPs, in addition to this group of proteins, may be required for the developement of thermotolerance.
Plant physiology, 1995
Examination of an ammonium sulfate-enriched fraction (70-1 00% saturation) of heat-shock proteins (HSPs) by nondenaturing polyacrylamide gel electrophoresis revealed the presence of a high molecular m a s complex (280 kD) in soybean (Glycine max) seedlings. This complex cross-reacted with antibodies raised against soybean class I low-molecular-mass (LMW) HSPs. Dissociation of the complex by denaturing polyacrylamide gel electrophoresis showed the complex to contain at least 15 polypeptides of the 15to 18-kD class I L M W HSPs that could be detected by staining, radiolabeling, and western blotting. A similar LMW-HSP complex was observed in mung bean (Vigna radiafa L.; 295 kD), in pea (Pisum safivum 1.; 270 kD), and in rice (Oryza sativa 1.; 310 kD). l h e complex was stable under high salt conditions (250 mM KCI), and the integrity was not affected by 1 % Nonidet P-40 and 3 & n L RNase treatment. l h e size of the isolated HSP complex in vitro was conserved to 55°C; however, starting at 37.5"C, it changed to higher molecular forms in the presence of soluble proteins. l h e isolated HSP complex was able to protect up to 75% of the soluble proteins from heat denaturation in vitro.
Heat Shock Proteins: Functions And Response Against Heat Stress In Plants
Heat stress has significant effect on protein metabolism, including degradation of proteins, inhibition of protein accumulation and induction of certain protein synthesis. It also poses a serious damage to the growth and development of the plant. The ability of the plants to respond to this stress by maintaining protein in their functional conformation as well as preventing the accumulation of non-native proteins are highly important for the cell survival. Heat shock proteins are involved in signaling, translation, host-defence mechanisms, carbohydrate metabolism and amino acid metabolism. In fact, these proteins are now understood to mediate signaling, translation, host-defence mechanisms, carbohydrate metabolism and amino acid metabolism by playing a significant function in controlling the genome and ultimately features that are obvious. Several reviews have reported the tolerance of plants to different abiotic stresses. The topic of enhancing protection mechanisms (including HSPs...
Heat shock triggers rapid protein phosphorylation in soybean seedings
Biochemical and Biophysical Research Communications, 1987
Heat shock arrests the synthesis of many cellular proteins and simultaneously initiates expression of a unique set of proteins, termed heat shock proteins. We have found that heat shock rapidly triggers phosphorylation of a set of proteins in soybean seedlings. Although the kinetics of phosphorylation and the heat shock response are similar, the major identified phosphorylation products do not comigrate with heat shock proteins on polyacrylamide gels. Cadmium, which is known to induce the heat shock response, stimulates phosphorylation of the same set of proteins. The rapidity of phosphorylation suggests that it may play a pivotal role in sensing and transducing elevated temperature stress in plants. m 1987 Academic Press, Inc.
Heat Shock Proteins and Heat Shock Response in Plants
gazi university journal of science, 2010
Normal 0 21 false false false TR X-NONE X-NONE MicrosoftInternetExplorer4 Prokaryotic and eukaryotic cells respond potentially harmful stimulations like heat stress by inducing synthesis of stress proteins so called heat shock proteins (Hsps) besides other metabolites. Heat stress response is a reaction when tissues and cells of an organism were exposed to sudden heat stress and is characterized by temporary expression of Hsps. Primary protein structures of Hsps and heat shock response are highly conserved in every organism which has been sought. Therefore it has been considered that Hsps might be closely involved in protection of organisms against heat stress and keeping homeostasis. Most of Hsps are known as molecular chaperons whose biological role is to maintain and shield the unfolded state of newly synthesized proteins thus preventing them from misfolding or aggregating. Here it was summarized the significance of Hsps and heat shock response in plants. Key Words : Heat stress...
Plant heat-shock proteins: A mini review
Journal of King Saud University-Science, 2011
Plants as sessile organisms are exposed to persistently changing stress factors. The primary stresses such as drought, salinity, cold and hot temperatures and chemicals are interconnected in their effects on plants. These factors cause damage to the plant cell and lead to secondary stresses such as osmotic and oxidative stresses. Plants cannot avoid the exposure to these factors but adapt morphologically and physiologically by some other mechanisms. Almost all stresses induce the production of a group of proteins called heat-shock proteins (Hsps) or stress-induced proteins. The induction of transcription of these proteins is a common phenomenon in all living things. These proteins are grouped in plants into five classes according to their approximate molecular weight: (1) Hsp100, (2) Hsp90, (3) Hsp70, (4) Hsp60 and (5) small heat-shock proteins (sHsps). Higher plants have at least 20 sHsps and there might be 40 kinds of these sHsps in one plant species. It is believed that this diversification of these proteins reflects an adaptation to tolerate the heat stress. Transcription of heat-shock protein genes is controlled by regulatory proteins called heat stress transcription factors (Hsfs). Plants show at least 21 Hsfs with each one having its role in regulation, but they also cooperate in all phases of periodical heat stress responses (triggering, maintenance and recovery). There are more than 52 plant species (including crop ones) that have been genetically engineered for different traits such as yield, herbicide and insecticide resistance and some metabolic changes.