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  • 1
    ISSN: 1432-2048
    Keywords: Regulation ; Hydrogen sulfide ; Sulfate reduction ; Adenosine-5′-phosphosulfate ; APS-sulfotransferase ; Lemna minor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When Lemna minor L. is transferred to an atmosphere with H2S, there is a rapid loss of extractable adenosine-5′-phosphosulfate sulfotransferase activity. The activity is restored within 24 h in an atmosphere without H2S. This restoration of activity is completely inhibited by cycloheximid but not by chloramphenicol. In vitro, S2- up to 5 mM and cysteine, methionine, and glutathione up to 50 mM do not inhibit the enzyme. The activities of ATP sulfurylase and O-acetyl-L-serine sulfhydrylase are not affected significantly by H2S. The physiological significance of the regulation of adenosine-5′-phosphosulfate sulfotransferase is discussed.
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  • 2
    ISSN: 1432-2048
    Keywords: Key words: Abscisic acid – Buthionine sulfoximine – Cysteine – Glutathione – Glutathione reductase –Zea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract.  The role of glutathione (GSH) in protecting plants from chilling injury was analyzed in seedlings of a chilling-tolerant maize (Zea mays L.) genotype using buthionine sulfoximine (BSO), a specific inhibitor of γ-glutamylcysteine (γEC) synthetase, the first enzyme of GSH synthesis. At 25 °C, 1 mM BSO significantly increased cysteine and reduced GSH content and GSH reductase (GR: EC 1.6.4.2) activity, but interestingly affected neither fresh weight nor dry weight nor relative injury. Application of BSO up to 1 mM during chilling at 5 °C reduced the fresh and dry weights of shoots and roots and increased relative injury from 10 to almost 40%. Buthionine sulfoximine also induced a decrease in GR activity of 90 and 40% in roots and shoots, respectively. Addition of GSH or γEC together with BSO to the nutrient solution protected the seedlings from the BSO effect by increasing the levels of GSH and GR activity in roots and shoots. During chilling, the level of abscisic acid increased both in controls and BSO-treated seedlings and decreased after chilling in roots and shoots of the controls and in the roots of BSO-treated seedlings, but increased in their shoots. Taken together, our results show that BSO did not reduce chilling tolerance of the maize genotype analyzed by inhibiting abscisic acid accumulation but by establishing a low level of GSH, which also induced a decrease in GR activity.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Planta 198 (1996), S. 139-143 
    ISSN: 1432-2048
    Keywords: Cadmium ; Copper ; Heavy-metal-binding peptides ; Phytochelatin ; Translocation (Cd, Cu) ; Zea (Cd, Cu transport)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Maize plants (Zea mays L. cv. Honeycomb F-1) were grown on quartz sand containing amounts of Cd or Cu which resulted in comparable internal contents in the roots. Fresh and dry weights and the content of Cd or Cu were measured in roots and shoots after eight weeks. In addition, cysteine, γ-glutamylcysteine (γEC), glutathione (GSH) and the thiols in heavy-metal-binding peptides (HMBPs) were determined in the roots. At low internal contents, Cd and Cu inhibited root growth to the same extent. Inhibition by Cu was enhanced, however, at high internal contents, indicating that Cu was more toxic than Cd. Separation of extracts from roots of Cd- and Cutreated plants on a Sephadex G-50 column resulted in HMBP complexes with relative molecular masses (Mrs) of 6200 and 7300, respectively. Separation of these HMBP-complexes using HPLC resulted in a distinct pattern of thiol compounds for each heavy metal. The accumulation of HMBPs was linearly dependent on the content of Cd at all values examined. In Cu-treated roots, HMBP accumulation was linearly dependent on the internal Cu content only up to 7.1 μmol·g−1 dry weight. At internal contents which caused an enhanced inhibition of root growth, no further significant increase in the HMBP content was detected. At these internal Cu contents an increased transport of Cu to the shoot was measured. This result indicates that HMBPs are involved in reducing heavy-metal transport from roots to shoots.
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  • 4
    ISSN: 1432-2048
    Keywords: Chilling ; Glutathione synthesis ; Sulfate reductionZea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effect of chilling on enzymes, substrates and products of sulfate reduction, gultathione synthesis and metabolism was studied in shoots and roots of maize (Zea mays L.) genotypes with different chilling sensitivity. At full expansion of the second leaf, chilling at 12 °C inhibited dry weight increase in shoots and roots compared to controls at 25 °C and induced an increase in adenosine 5′-phosphosulfate sulfotransferase and γ-glutamylcysteine synthetase (EC 6.3.2.2) activity in the second leaf of all genotypes tested. Glutathione synthetase (EC 6.3.2.3) activity was about one order of magnitude higher than γ-glutamylcysteine synthetase activity, but remained unchanged during chilling except for one genotype. During chilling, cysteine and glutathione content of second leaves increased to significantly higher levels in the two most chilling-tolerant genotypes. Comparing the most tolerant and most sensitive genotype showed that chilling induced a greater incorporation of35S from [35S]sulfate into cysteine and glutathione in the chilling-tolerant than in the sensitive genotype. Chilling decreased the amount of35S-label incorporated into proteins in shoots of both genotypes, but had no effect on this incorporation in the roots. Glutathione reductase (EC 1.6.4.2) and nitrate reductase (EC 1.6.6.1) activity were constitutively higher in the chilling-tolerant genotypes, but showed no changes in most examined genotypes during 3 d at 12 °C. Our results indicate that in maize glutathione is involved in protection against chilling damage.
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  • 5
    ISSN: 1432-2048
    Keywords: Adenosine 5′-phosphosulfate sulfotransferase ; Lemna ; sulfate assimilation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The role of de novo synthesis in the regulation of adenosine 5′-phosphosulfate sulfotransferase activity by H2S inLemna minor L. was investigate using density labeling with15N applied as15NO 3 − in the culture medium. While adenosine 5′-phosphosulfate sulfotransferase activity was rapidly reduced by H2S and rapidly recovered upon removal of H2S, O-acetyl-L-serine sulfhydrylase (EC 4.2.99.8) did not show changes in extractable activity in response to H2S and could therefore be used as an internal marker enzyme for density labeling. The incorporation of15N into adenosine 5′-phosphosulfate sulfotransferase was strongly reduced upon transfer of plants into a H2S-containing atmosphere. Half-maximal labeling was reached only after 70–80 h compared to 40–50 h in the control. After removal of H2S, adenosine 5′-phosphosulfate sulfotransferase activity increased to the initial level within 20 h, and the enzyme reached halfmaximal labeling after only 15 h. The time course of the density increase of O-acetyl-L-serine sulfhydrylase was not affected very significantly by H2S. These results provide evidence that de novo synthesis of enzyme protein is involved in the regulation of adenosine 5′-phosphosulfate sulfotransferase activity by H2S.
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Planta 143 (1978), S. 285-289 
    ISSN: 1432-2048
    Keywords: Adenosine 5′-phosphosulfate sulfotransferase ; Chloroplasts ; Spinacia sulfate reduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Roots of spinach (Spinacia oleracea L.) seedlings contained only a very low activity of adenosine 5′-phosphosulfate sulfotransferase compared to the cotyledons. Adenosine 5′-phosphosulfate sulfotransferase activity increased about tenfold in cotyledons during greening. Preparation of organelle fractions from spinach leaves by a combination of differential and isopycnic density gradient centrifugation showed that adenosine 5′-phosphosulfate sulfotransferase banded with NADP-glyceraldehyde-3-phosphate dehydrogenase, a marker enzyme for intact chloroplasts. In the fractions of peroxisomes, mitochondria and broken chloroplasts virtually no adenosine 5′-phosphosulfate sulfotransferase activity was measured. Comparison with the chloroplast enzyme NADP-glyceraldehyde-3-phosphate dehydrogenase indicates that in spinach, adenosine 5′-phosphosulfate sulfotransferase is localized almost exclusively in the chloroplasts.
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  • 7
    ISSN: 1432-2048
    Keywords: Adenosine 5′-phosphosulfate sulfotransferase ; Cysteine ; Phaseolus ; Sulfide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract During chloroplast development in the primary leaves of Phaseolus vulgaris, the extractable activity of adenosine 5′-phosphosulfate sulfotransferase increased ten-fold. When chloroplast development took place in air enriched with 3.5 μl H2S·l-1 there was a decrease in adenosine 5′-phosphosulfate sulfotransferase activity. Cyst(e)ine in concentrations up to 1 mM (in the external medium) did not affect the increase in adenosine 5′-phosphosulfate sulfotransferase activity in intact plants. In plants with excised roots, 0.75 mM cyst(e)ine inhibited this increase. In green primary leaves, H2S or cyst(e)ine treatment resulted in a decrease of extractable adenosine 5′-phosphosulfate sulfotransferase activity. In intact plants, this effect of cyst(e)ine was observed at a concentration of 1 mM, and in plants with excised roots, 0.25 mM had a comparable effect. In developing plants, the extractable activities of O-acetyl-L-serine sulfhydrylase (EC 4.2.99.9) and ribulosebisphosphate carboxylase (EC 4.1.1.39.) were not affected by H2S or cyst(e)ine.
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  • 8
    ISSN: 1617-4623
    Keywords: Protoplast fusion ; Nitrate reductase deficiency ; Kanamycin ; Nicotiana tabacum ; Nicotiana sylvestris
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The combination in the nuclear genome of a dominant resistance marker (to select against unfused wild-type cells) and a recessive deficiency marker (to select against unfused mutant cells) in a cell line should provide a system for selecting fusion hybrids between the mutant line and any wild-type line. To test this idea, we fused protoplasts from a non-morphogenic cell line of Nicotiana tabacum which was kanamycin resistant (by transformation) and deficient in nitrate reductase (NR-K+) with protoplasts from N. tabacum cv. Petit Havana clone SR1, which provided resistance against streptomycin as an additional selectable marker (NR+K-SR+). Putative hybrids were selected using a culture medium containing no available reduced nitrogen source and 50 mg/l kanamycin sulphate. After regeneration into plants, the hybrid character was demonstrated from: (i) the morphological variation of the regenerants; (ii) the chromosome number; (iii) the ability to grow on medium without a reduced nitrogen source and containing kanamycin sulphate at 50 mg/l; (iv) the presence of nitrate reductase activity; (v) the presence of the gene coding for neomycin phosphotransferase, which provides resistance to kanamycin sulphate; (vi) callus formation from leaves on medium containing 1 g/l streptomycin or 50 mg/l kanamycin sulphate; (vii) F1 plants containing nitrate reductase and the gene for neomycin phosphotransferase. Fusions between the mutant cell line (NR-K+) and three wild-type tobacco species and subsequent cultivation on medium containing no available nitrogen source but 50 mg/l kanamycin sulphate resulted in callus formation with all combinations, while hybrid plants were only regenerated when N. sylvestris was the fusion partner.
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  • 9
    Publication Date: 1980-01-01
    Print ISSN: 0032-0935
    Electronic ISSN: 1432-2048
    Topics: Biology
    Published by Springer
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  • 10
    Publication Date: 1978-01-01
    Print ISSN: 0032-0935
    Electronic ISSN: 1432-2048
    Topics: Biology
    Published by Springer
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