Induction and Accumulation of Heat Shock-Specific Poly(A<sup>+</sup>) RNAs and Proteins in Soybean Seedlings during Arsenite and Cadmium Treatments

Edelman, Leonard; Czarnecka, Eva; Key, Joe L.

doi:10.1104/pp.86.4.1048

Cited by 46 publications

(23 citation statements)

References 27 publications

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“…As found in several studies of hsp genes in soybean and petunia (6,8,9,28), arsenite and cadmium ions affected the expression of hsp genes in Arabidopsis. In petunia leaves, treatment with 0.05 mM CdCl2 clearly increases the level of hsp7O mRNA and also causes accumulation of a nonprocessed precursor (28).…”

Section: Comparison Of the Expression Of The Hsp Genes In Arabidopsismentioning

confidence: 51%

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Isolation and Analysis of the Expression of Two Genes for the 81-Kilodalton Heat-Shock Proteins from Arabidopsis

Takahashi¹,

Naito²,

Komeda³

1992

Plant Physiol.

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We have cloned and characterized two members of the family of genes for the 81-kilodalton heat-shock proteins from Arabidopsis thaliana, HSP81-1 and HSP81-2. Comparison of the entire genomic sequence of the HSP81-1 gene with the corresponding full-length cDNA previously reported as AtHS83 (TW Conner, PR LaFayette, RT Nagao, JL Key [1990] Plant Physiol 94: 1689-1695 reveals the presence of three introns of 315, 83, and 88 base pairs. By contrast, analysis of the HSP81-2 genomic and partial cDNA sequences suggests that the HSP81-2 gene is interrupted by only two introns of 304 and 106 base pairs. The 5'-initiation sites of the two corresponding mRNAs were mapped from results of experiments with SI nuclease. The deduced amino acid sequences of the proteins encoded by these two genes show 88% identity, and they also show striking similarities to the hsp90 family of proteins in yeast and animal cells. From the results of northem blot analysis of transcripts, it appears that the expression of the HSP81-1 gene occurs at only very low levels in the absence of heat shock and is strongly induced by heat (350C).The HSP81-2 gene is constitutively expressed at much higher levels, and its expression is moderately enhanced by elevated temperatures. Severe heat shock appears to block the splicing of the pre-mRNA transcribed from HSP81-1. We also examined the effects of arsenite and cadmium on the expression of the HSP81 genes, as well as on other groups of hsp genes in Arabidopsis. Treatment with cadmium was marginally effective in inducing hsp genes, whereas arsenite stress strongly stimulated the accumulation of each mRNA in a coordinated fashion. transcriptional level. Nucleotide sequence analysis of plant hsp genes has revealed the presence of a positive control element (25) that is homologous to the HSE, which was originally identified upstream of the hsp genes in Drosophila (19). This finding suggests that, in plants, transcriptional regulation of hsp genes is mediated by the binding to HSEs of trans-acting factors, referred to as heat-shock factors, in a similar way to that reported for other eukaryotes, such as fruit flies, yeast cells, and HeLa cells (32).The expression of hsp genes in plants is also induced by adverse environmental stimuli other than heat shock. These stimuli include heavy metal ions, arsenite, phytohormones (6,8,9,28), and insecticides (22). The regulation of hsp genes has also been shown to be dependent on the developmental stage of the plant (27). However, the molecular mechanisms of plant responses to a wide range of stresses and the physiological significance of hsps under stressed conditions remain obscure.As an initial approach to resolving these issues, we previously isolated and characterized two genes that encode small hsps in Arabidopsis thaliana (26). We have now extended our analysis of the hsp genes from Arabidopsis and report here the cloning of two distinct members of the family of genes for 81 -kD hsps, as well as their complete nucleotide sequences. Examination of the ups...

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Section: Comparison Of the Expression Of The Hsp Genes In Arabidopsismentioning

confidence: 51%

“…These stimuli include heavy metal ions, arsenite, phytohormones (6,8,9,28), and insecticides (22). The regulation of hsp genes has also been shown to be dependent on the developmental stage of the plant (27).…”

Section: Introductionmentioning

confidence: 99%

Isolation and Analysis of the Expression of Two Genes for the 81-Kilodalton Heat-Shock Proteins from Arabidopsis

Takahashi¹,

Naito²,

Komeda³

1992

Plant Physiol.

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“…5B, lane 4). Since arsenite and the amino acid analogs azetidine or canavanine were shown to induce synthesis of a whole family of HSPs at 28°C in soybean (Lin et al, 1984;Edelman et al, 1988;Nover, 1990), we examined the formation of the HMW complex under these treatments. It is clear, as shown in Figure 6, lanes 2, 3, and 4, that the size of the higherorder structure formed during stress treatments with these chemicals at 28°C was the same as that formed during HS (shown in lane 1).…”

Section: The Mass Of the Class I Lmw-hsp Complex During Recoverymentioning

confidence: 99%

Characterization and Physiological Function of Class I Low-Molecular-Mass, Heat-Shock Protein Complex in Soybean

1995

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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 15-to 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.The induction of HSP synthesis in response to thermal stress occurs in a11 organisms that have been examined, ranging from bacteria to humans (Schlesinger et al., 1982;Vierling, 1991). Whereas the physiological functions of HSPs have not been clearly established, these proteins are well correlated with the acquisition of thermotolerance in a time-and temperature-dependent manner. Under HS conditions the expression of the LMW HSPs in soybean (Glycine max) is increased, yielding final concentrations of up to 1% of the total cellular proteins (Hsieh et al., 1992). Based on this correlation, it has been hypothesized that accumulation of HSPs is a n essential component of a process that prevents heat damage (Lin et al., 1984;Key et al., 1985;Kimple et al., 1990). Some HSPs become selectively localized in cellular organelles in a temperature-dependent fashion and relocate to the cytoplasm after a 28°C incubation period (Lin et al., 1984). Isolated mitochondria with associated HSPs are functional in oxidative phosphorylation under thermal stress, suggesting that association of HSPs with organelles provide protection from heat damage (Chou et al., 1989 (Jinn et al., 1993). In soybean, depletion of the 15-to 18-kD HSPs in the HSP-enriched fraction resulted in the loss of the thermostabilizing ability, and this ability was again restored when these HSPs were added. The protection provided by these HSP-enriched fractions is effective mainly for membrane-associated proteins (Jinn et al., 1993).The LMW HSPs of plants and a11 other eukaryotes have a conserved carboxyl-terminal region homologous to the a-crystallin of the eye lens at the amino acid sequence leve1 (Ingolia and Craig, 1982; Augusteyn and Koretz, 1987;Lindquist and Craig, 1988). The LMW HSPs in vertebrates (Arrigo and Welch, 1987;Merck et al., 1993), Drosopkila (Arrigo and Pauli, 1988), ye...

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“…However, the mechanisms which govern gene expression during stress and the biological significance of the stress-induced proteins are not well understood. A few cases are known in which exposure to a certain stress has been found to induce protein responses typical of another stress (3,6) or even tolerance to another stress (9). This indicates that a certain commonality exists between responses to different stresses, and yet, individual stresses also induce a unique response.…”

mentioning

confidence: 99%

Comparative analysis of proteins induced by heat shock, salinity, and osmotic stress in the nitrogen-fixing cyanobacterium Anabaena sp. strain L-31

Bhagwat

Apte

1989

J Bacteriol

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Heat, salinity, or osmotic stress influenced protein synthesis in nitrogen-fixing Anabaena sp. strain L-31.Salinity and osmotic stresses were identical and specifically induced 15 polypeptides. Four polypeptides were unique to heat shock, and four other polypeptides were induced under every stress. The results demonstrate a commonality and a stress specificity of protein synthesis regulation.Environmental-stress-induced modifications of protein synthesis have been observed in microbes, plants, and animals (3,7,10,(12)(13)(14) Preparation of total-cellular-protein samples, sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and two-dimensional electrophoresis (isoelectric focusing followed by SDS-PAGE) were performed as previously described (1,11). Only the reproducible and prominent differences were taken into account.Exposure to heat, salinity, or osmotic stress resulted in alterations in cyanobacterial-protein syntheses (Fig. 1). Three prominent types of modifications were noted: (i) synthesis of several proteins declined, (ii) synthesis of certain other proteins was selectively enhanced, and (iii) synthesis of a new set of proteins was induced de novo. Some of these responses were observed under all stress conditions (tentatively called the common-stress proteins), while others were found to be specific to either heat (heat shock proteins) or salinity/osmotic stress (osmotic-stress proteins).Two-dimensional separation of stress-modulated proteins (Fig. 2) further resolved protein synthesis responses and identified additional polypeptides which could not be visualized by SDS-PAGE (Fig. 1) of 23, 21, 20, 19, 18.5, and 18 kDa) were specifically induced only under salinity/osmotic stress, while induction of 4 proteins (92, 75, 65, and 32 kDa) were restricted to heat shock. The responses of protein synthesis to salt stress and osmotic stress were identical, indicating that the salinity stress-induced proteins previously reported (1) were all a result of osmotic stress per se and that the effect of ionic stress, if any, was negligible. This also explains our earlier observation that the cyanobacterial salinity stress-induced proteins could be induced externally

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Induction and Accumulation of Heat Shock-Specific Poly(A⁺) RNAs and Proteins in Soybean Seedlings during Arsenite and Cadmium Treatments

Cited by 46 publications

References 27 publications

Isolation and Analysis of the Expression of Two Genes for the 81-Kilodalton Heat-Shock Proteins from Arabidopsis

Isolation and Analysis of the Expression of Two Genes for the 81-Kilodalton Heat-Shock Proteins from Arabidopsis

Characterization and Physiological Function of Class I Low-Molecular-Mass, Heat-Shock Protein Complex in Soybean

Comparative analysis of proteins induced by heat shock, salinity, and osmotic stress in the nitrogen-fixing cyanobacterium Anabaena sp. strain L-31

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Induction and Accumulation of Heat Shock-Specific Poly(A+) RNAs and Proteins in Soybean Seedlings during Arsenite and Cadmium Treatments

Cited by 46 publications

References 27 publications

Isolation and Analysis of the Expression of Two Genes for the 81-Kilodalton Heat-Shock Proteins from Arabidopsis

Isolation and Analysis of the Expression of Two Genes for the 81-Kilodalton Heat-Shock Proteins from Arabidopsis

Characterization and Physiological Function of Class I Low-Molecular-Mass, Heat-Shock Protein Complex in Soybean

Comparative analysis of proteins induced by heat shock, salinity, and osmotic stress in the nitrogen-fixing cyanobacterium Anabaena sp. strain L-31

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Induction and Accumulation of Heat Shock-Specific Poly(A⁺) RNAs and Proteins in Soybean Seedlings during Arsenite and Cadmium Treatments