Isolation and Partial Characterization of a Cadmium-binding Protein from Pisum sativum

Grünhage, Ludger; Weigel, Hans‐Joachim; Ilge, D.; Jäger, Hans‐Jürgen

doi:10.1016/s0176-1617(85)80100-0

Cited by 23 publications

(4 citation statements)

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“…It is well known that specific molecules such as phytochelatins and stress proteins play a very significant role in Cd detoxification and/or tolerance in plants (Sanità di Toppi & Gabbrielli, 1999; Cobbett, 2000). A Cd‐binding protein and a gene with homology to some metallothionein genes have been isolated from Cd‐exposed pea plants (Grünhage et al ., 1985; Evans et al ., 1990) and Cd effects on glutathione and phytochelatin synthesis have been reported in pea (Rüegsegger et al ., 1990; Klapheck et al ., 1994).…”

Section: Introductionmentioning

confidence: 99%

Targeted proteomics to identify cadmium‐induced protein modifications in Glomus mosseae‐inoculated pea roots

Bestel-Corre²,

et al. 2003

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Summary• Arbuscular mycorrhiza (AM) can increase plant tolerance to heavy metals. A targeted proteomic approach was used to determine the putative identity of some of the proteins induced/modulated by cadmium (Cd) and to analyse the impact of the mycorrhizal process.• The effect of Cd (100 mg Cd kg − 1 substrate) applied either at planting or 15 d later on two pea ( Pisum sativum ) genotypes, differing in sensitivity to Cd inoculated or not with the AM fungus Glomus mosseae , was studied at three levels: plant biomass production, development of G. mosseae and root differential protein display with one-and two-dimensional gel electrophoresis (1-DE and 2-DE) analyses.• Cd-induced growth inhibition was significantly alleviated by mycorrhiza in the Cd-sensitive genotype. The AM symbiosis modulated the expression of several proteins, identified by liquid chromatography-tandem mass spectrometry, newly induced and upregulated or downregulated by Cd.• The protective effect of AM symbiosis towards Cd stress was observed in the Cdsensitive genotype. Our results demonstrate the usefulness of proteomics to better understand the possible role of AM symbiosis in detoxification/response mechanisms towards Cd in pea plants.

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Section: Introductionmentioning

confidence: 99%

Targeted proteomics to identify cadmium‐induced protein modifications in Glomus mosseae‐inoculated pea roots

Bestel-Corre²,

et al. 2003

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“…A similar dependence has been noted for metallothioneins (22). We conclude that the molecular weight of the native metal-containing phytochelatin complex is 2000-4000 (23-26), rather than the %10,000 observed at low ionic strength (13,(15)(16)(17)(18)(19)(20)(21). We reexamined the heavy metal metabolism in S. cucubalus (19) and A. tenuis (23) cell cultures, as well as in plants of L. esculentum (26) and Z. mayst.…”

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confidence: 96%

Phytochelatins, a class of heavy-metal-binding peptides from plants, are functionally analogous to metallothioneins

Grill

Winnacker²,

Zenk

1987

Proc. Natl. Acad. Sci. U.S.A.

744

433

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Phytochelatins are a class of heavy-metalbinding peptides previously isolated from cell suspension cultures of several dicotyledonous and monocotyledonous plants. These peptides consist of repetitive y-glutamylcysteine units with a carboxyl-terminal glycine and range from 5 to 17 amino acids in length. In the present paper we show that all plants tested synthesized phytochelatins upon exposure to heavy metal ions. No evidence for the occurrence of metallothionein-like proteins was found. All data so far obtained indicate that phytochelatins are involved in detoxification and homeostasis of heavy metals in plants and thus serve functions analogous to those of metallothioneins in animals and some fungi. Phytochelatins are induced by a wide range of metal anions and cations. Phytochelatin synthesis in suspension cultures was inhibited by buthionine sulfoximine, a specific inhibitor of y-glutamylcysteine synthetase (EC 6.3.2.2). This finding and kinetic studies of phytochelatin induction point to a synthesis from glutathione or its precursor, r-glutamylcys-

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“…In higher plants the inducible Cd-binding compounds showed properties distinctly different from metallothioneins: in Ouchterlony two-dimensional immunodiffusion tests, no cross-reaction could be observed (7), and attempts to establish the primary structure by Edman degradation failed (5). Similarities were a high cysteine content, A254:A280> 1, and comparable circular dichroism spectra (5), indicating the lack of aromatic residues and the possible binding of heavy metals by mercaptide complexes.…”

mentioning

confidence: 99%

Regulation of Assimilatory Sulfate Reduction by Cadmium in Zea mays L.

Nussbaum¹,

Schmutz²,

Brunold³

1988

Plant Physiol.

159

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Plants cultivated with Cd can produce large amounts of phytochelatins. Since these compounds contain much cysteine, these plants should have an increased rate of assimilatory sulfate reduction, the biosynthetic pathway leading to cysteine. To test this prediction, the effect of Cd on growth, sulfate assimilation in vivo and extractable activity of two enzymes of sulfate reduction, ATP-sulfurylase (EC 2.7.7.4) and adenosine 5'-phosphosulfate sulfotransferase were measured in maize (Zea mays L.) seedlings. For comparison, nitrate reductase activity was determined. In 9-day-old cultures, the increase in fresh and dry weight was significantly inhibited by 50 micromolar and more Cd in the roots and by 100 and 200 micromolar in the shoots. Seedlings cultivated with 50 micromolar Cd for 5 days incorporated more label from 35SO42-into higher molecular weight compounds than did controls, indicating that the predicted increase in the rate of assimilatory sulfate reduction took place. Consistent with this finding, an increased level of the extractable activity of both ATP-sulfurylase and adenosine 5'-phosphosulfate sulfotransferase was measured in the roots of these plants at 50 micromolar Cd and at higher concentrations. This effect was reversible after removal of Cd from the nutrient solution. In the leaves, a significant positive effect of Cd was detected at 5 micromolar for ATP-sulfurylase and at 5 and 20 micromolar for adenosine 5'-phosphosulfate sulfotransferase. At higher Cd concentrations, both enzyme activities were at levels below the control. Nitrate reductase (EC 1.6.6.1) activity decreased at 50 micromolar or more Cd in the roots and was similarly affected as ATP-sulfurylase activity in the primary leaves.In 1957 a cysteine-rich, Cd-binding protein was isolated from equine kidney (10) and subsequently called metallothionein. In higher plants the inducible Cd-binding compounds showed properties distinctly different from metallothioneins: in Ouchterlony two-dimensional immunodiffusion tests, no cross-reaction could be observed (7), and attempts to establish the primary structure by Edman degradation failed (5). Similarities were a high cysteine content, A254:A280> 1, and comparable circular dichroism spectra (5), indicating the lack of aromatic residues and the possible binding of heavy metals by mercaptide complexes.

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Isolation and Partial Characterization of a Cadmium-binding Protein from Pisum sativum

Cited by 23 publications

References 20 publications

Targeted proteomics to identify cadmium‐induced protein modifications in Glomus mosseae‐inoculated pea roots

Targeted proteomics to identify cadmium‐induced protein modifications in Glomus mosseae‐inoculated pea roots

Phytochelatins, a class of heavy-metal-binding peptides from plants, are functionally analogous to metallothioneins

Regulation of Assimilatory Sulfate Reduction by Cadmium in Zea mays L.

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