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Publikationen - Stress- und Entwicklungsbiologie

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Publikation

Leopold, I.; Günther, D.; Schmidt, J.; Neumann, D.; Phytochelatins and heavy metal tolerance Phytochemistry 50, 1323-1328, (1999) DOI: 10.1016/S0031-9422(98)00347-1

The induction and heavy metal binding properties of phytochelatins in heavy metal tolerant (Silene vulgaris) and sensitive (tomato) cell cultures, in water cultures of these plants and in Silene vulgaris grown on a medieval copper mining dump were investigated. Application of heavy metals to cell suspension cultures and whole plants of Silene vulgaris and tomato induces the formation of heavy metal–phytochelatin-complexes with Cu and Cd and the binding of Zn and Pb to lower molecular weight substances. The binding of heavy metal ions to phytochelatins seems to play only a transient role in the heavy metal detoxification, because the Cd- and Cu-complexes disappear in the roots of water cultures of Silene vulgaris between 7 and 14 days after heavy metal exposition. Free heavy metal ions were not detectable in the extracts of all investigated plants and cell cultures. Silene vulgaris plants grown under natural conditions on a mining dump synthesize low molecular weight heavy metal binding compounds only and show no complexation of heavy metal ions to phytochelatins. The induction of phytochelatins is a general answer of higher plants to heavy metal exposition, but only some of the heavy metal ions are able to form stable complexes with phytochelatins. The investigation of tolerant plants from the copper mining dump shows that phytochelatins are not responsible for the development of the heavy metal tolerant phenotypes.
Publikation

Clemens, S.; Kim, E. J.; Neumann, D.; Schroeder, J. I.; Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast EMBO J. 18, 3325-3333, (1999) DOI: 10.1093/emboj/18.12.3325

Phytochelatins play major roles in metal detoxification in plants and fungi. However, genes encoding phytochelatin synthases have not yet been identified. By screening for plant genes mediating metal tolerance we identified a wheat cDNA, TaPCS1 , whose expression in Saccharomyces cerevisiae results in a dramatic increase in cadmium tolerance. TaPCS1 encodes a protein of ∼55 kDa with no similarity to proteins of known function. We identified homologs of this new gene family from Arabidopsis thaliana , Schizosaccharomyces pombe , and interestingly also Caenorhabditis elegans . The Arabidopsis and S.pombe genes were also demonstrated to confer substantial increases in metal tolerance in yeast. PCS‐expressing cells accumulate more Cd2+ than controls. PCS expression mediates Cd2+ tolerance even in yeast mutants that are either deficient in vacuolar acidification or impaired in vacuolar biogenesis. PCS‐induced metal resistance is lost upon exposure to an inhibitor of glutathione biosynthesis, a process necessary for phytochelatin formation. Schizosaccharomyces pombe cells disrupted in the PCS gene exhibit hypersensitivity to Cd2+ and Cu2+ and are unable to synthesize phytochelatins upon Cd2+ exposure as determined by HPLC analysis. Saccharomyces cerevisiae cells expressing PCS produce phytochelatins. Moreover, the recombinant purified S.pombe PCS protein displays phytochelatin synthase activity. These data demonstrate that PCS genes encode phytochelatin synthases and mediate metal detoxification in eukaryotes.
Publikation

Bringezu, K.; Lichtenberger, O.; Leopold, I.; Neumann, D.; Heavy Metal Tolerance of Silene vulgaris J. Plant Physiol. 154, 536-546, (1999) DOI: 10.1016/S0176-1617(99)80295-8

Silene vulgaris ssp. humilis, a heavy metal tolerant plant growing on the polluted soil of a medieval copper mining dump, accumulates considerable amounts of heavy metals (HM) in its roots and shoots. The intracellular distribution of HMs in the leaves was investigated by conventional and analytical (EDX, ESI, EELS) electron microscopy. Part of the HMs, Fe, Cu, and Zn occur as crystalline compounds on the surface of the leaves. The epidermal cell walls accumulate Fe, Ni, Cu, AI, Sn, and Zn. Cu within the cell walls is tightly bound to a protein with oxalate oxidase activity, evidencing a high homology to germin. Zn and Sn are accumulated in the cell walls as silicate. Cytoplasm and organelles contain only traces of Cu and Sn, while in the vacuoles no HMs are detected. In the epidermal cell walls, intercellular spaces, and in vacuoles there are high concentrations of Si, forming crystal-like structures. EELS and quantum-chemical calculations reveal these structures as SiO2. The role of Si in the HM-tolerance of Silene is discussed.
Publikation

Baizabal-Aguirre, V. M.; Clemens, S.; Uozumi, N.; Schroeder, J. I.; Suppression of Inward-Rectifying K+ Channels KAT1 and AKT2 by Dominant Negative Point Mutations in the KAT1 α-Subunit J. Membr. Biol. 167, 119-125, (1999) DOI: 10.1007/s002329900476

The Arabidopsis thaliana cDNA, KAT1 encodes a hyperpolarization-activated K+ (K+ in ) channel. In the present study, we identify and characterize dominant negative point mutations that suppress K+ in channel function. Effects of two mutations located in the H5 region of KAT1, at positions 256 (T256R) and 262 (G262K), were studied. The co-expression of either T256R or G262K mutants with KAT1 produced an inhibition of K+ currents upon membrane hyperpolarization. The magnitude of this inhibition was dependent upon the molar ratio of cRNA for wild-type to mutant channel subunits injected. Inhibition of KAT1 currents by the co-expression of T256R or G262K did not greatly affect the ion selectivity of residual currents for Rb+, Na+, Li+, or Cs+. When T256R or G262K were co-expressed with a different K+ channel, AKT2, an inhibition of the channel currents was also observed. Voltage-dependent Cs+ block experiments with co-expressed wild type, KAT1 and AKT2, channels further indicated that KAT1 and AKT2 formed heteromultimers. These data show that AKT2 and KAT1 are able to co-assemble and suggest that suppression of channel function can be pursued in vivo by the expression of the dominant negative K + in channel mutants described here.
Publikation

Clemens, S.; Antosiewicz, D. M.; Ward, J. M.; Schachtman, D. P.; Schroeder, J. I.; The plant cDNA LCT1 mediates the uptake of calcium and cadmium in yeast Proc. Natl. Acad. Sci. U.S.A. 95, 12043-12048, (1998) DOI: 10.1073/pnas.95.20.12043

Nonessential metal ions such as cadmium are most likely transported across plant membranes via transporters for essential cations. To identify possible pathways for Cd2+ transport we tested putative plant cation transporters for Cd2+ uptake activity by expressing cDNAs in Saccharomyces cerevisiae and found that expression of one clone, LCT1, renders the growth of yeast more sensitive to cadmium. Ion flux assays showed that Cd2+ sensitivity is correlated with an increase in Cd2+ uptake. LCT1-dependent Cd2+ uptake is saturable, lies in the high-affinity range (apparent KM for Cd2+ = 33 μM) and is sensitive to block by La3+ and Ca2+. Growth assays demonstrated a sensitivity of LCT1-expressing yeast cells to extracellular millimolar Ca2+ concentrations. LCT1-dependent increase in Ca2+ uptake correlated with the observed phenotype. Furthermore, LCT1 complements a yeast disruption mutant in the MID1 gene, a non-LCT1-homologous yeast gene encoding a membrane Ca2+ influx system required for recovery from the mating response. We conclude that LCT1 mediates the uptake of Ca2+ and Cd2+ in yeast and may therefore represent a first plant cDNA encoding a plant Ca2+ uptake or an organellar Ca2+ transport pathway in plants and may contribute to transport of the toxic metal Cd2+ across plant membranes.
Publikation

Vörös, K.; Feussner, I.; Kühn, H.; Lee, J.; Graner, A.; Löbler, M.; Parthier, B.; Wasternack, C.; Characterization of a methyljasmonate-inducible lipoxygenase from barley (Hordeum vulgare cv. Salome) leaves Eur. J. Biochem. 251, 36-44, (1998) DOI: 10.1046/j.1432-1327.1998.2510036.x

We found three methyl jasmonate−induced lipoxygenases with molecular masses of 92 kDa, 98 kDa, and 100 kDa (LOX‐92, ‐98 and ‐100) [Feussner, I., Hause, B., Vörös, K., Parthier, B. & Wasternack, C. (1995) Plant J. 7 , 949−957]. At least two of them (LOX‐92 and LOX‐100), were shown to be localized within chloroplasts of barley leaves. Here, we describe the isolation of a cDNA (3073 bp) coding for LOX‐100, a protein of 936 amino acid residues and a molecular mass of 106 kDa. By sequence comparison this lipoxygenase could be identified as LOX2‐type lipoxygenase and was therefore designated LOX2 : Hv : 1 . The recombinant lipoxygenase was expressed in Escherichia coli and characterized as linoleate 13‐LOX and arachidonate 15‐LOX, respectively. The enzyme exhibited a pH optimum around pH 7.0 and a moderate substrate preference for linoleic acid. The gene was transiently expressed after exogenous application of jasmonic acid methyl ester with a maximum between 12 h and 18 h. Its expression was not affected by exogenous application of abscisic acid. Also a rise of endogenous jasmonic acid resulting from sorbitol stress did not induce LOX2 : Hv : 1 , suggesting a separate signalling pathway compared with other jasmonate‐induced proteins of barley. The properties of LOX2 : Hv : 1 are discussed in relation to its possible involvement in jasmonic acid biosynthesis and other LOX forms of barley identified so far.
Publikation

Schmidt, A.; Scheel, D.; Strack, D.; Elicitor-stimulated biosynthesis of hydroxycinnamoyltyramines in cell suspension cultures of Solanum tuberosum Planta 205, 51-55, (1998) DOI: 10.1007/s004250050295

Treatment of suspension-cultured potato cells (Solanum tuberosum L. cv. Desirée) with an elicitor from Phytophthora infestans induced increased incorporation of 4-hydroxybenzaldehyde, 4-hydroxybenzoate, and N-4-coumaroyl- and N-feruloyltyramine into the cell␣wall and secretion of N-4-coumaroyl- and N-feruloyltyramine into the culture medium. Induced metabolite accumulation was preceded by rapid and transient increases in activities of phenylalanine ammonia-lyase (EC 4.3.1.5) and tyrosine decarboxylase (TyrDC; EC 4.1.1.25), exhibiting maximal activities 5–10 h after initiation of elicitor treatment. Activities of hydroxycinnamoyl-CoA:tyramine hydroxycinnamoyltransferase (EC 2.3.1.110), catalyzing the formation of N-4-coumaroyl- and N-feruloyltyramine, increased later and remained at high levels. The phenolic defense compounds appear to be involved in cell wall reinforcement and may further directly affect fungal growth in the apoplastic space.
Publikation

Scheel, D.; Resistance response physiology and signal transduction Curr. Opin. Plant Biol. 1, 305-310, (1998) DOI: 10.1016/1369-5266(88)80051-7

Plants defend themselves against pathogen attack by activating a multicomponent defense response. The activation of this response requires recognition of the pathogen and initiation of signal transduction processes that finally result in a spatially and temporally regulated expression of individual defense reactions. Several components involved in signaling resistance reactions have recently been identified and characterized.
Publikation

Nennstiel, D.; Scheel, D.; Nürnberger, T.; Characterization and partial purification of an oligopeptide elicitor receptor from parsley (Petroselinum crispum) FEBS Lett. 431, 405-410, (1998) DOI: 10.1016/S0014-5793(98)00800-X

Parsley cells recognize the fungal phytopathogen Phytophthora sojae through a plasma membrane receptor. A 13 amino acid oligopeptide fragment (Pep-13) of a 42 kDa fungal cell wall glycoprotein was shown to bind to the receptor and stimulate a complex defense response in cultured parsley cells. The Pep-13 binding site solubilized from parsley microsomal membranes by non-ionic detergents exhibited the same ligand affinity and ligand specificity as the membrane-bound receptor. Chemical crosslinking and photoaffinity labeling assays with [125I]Pep-13 revealed that a monomeric 100 kDa integral plasma membrane protein is sufficient for ligand binding and may thus constitute the ligand binding domain of the receptor. Ligand affinity chromatography of solubilized microsomal membrane protein on immobilized Pep-13 yielded a 5000-fold enrichment of specific receptor activity.
Publikation

Zimmermann, S.; Nürnberger, T.; Frachisse, J.-M.; Wirtz, W.; Guern, J.; Hedrich, R.; Scheel, D.; Receptor-mediated activation of a plant Ca2+-permeable ion channel involved in pathogen defense Proc. Natl. Acad. Sci. U.S.A. 94, 2751-2755, (1997) DOI: 10.1073/pnas.94.6.2751

Pathogen recognition at the plant cell surface typically results in the initiation of a multicomponent defense response. Transient influx of Ca2+ across the plasma membrane is postulated to be part of the signaling chain leading to pathogen resistance. Patch-clamp analysis of parsley protoplasts revealed a novel Ca2+-permeable, La3+-sensitive plasma membrane ion channel of large conductance (309 pS in 240 mM CaCl2). At an extracellular Ca2+ concentration of 1 mM, which is representative of the plant cell apoplast, unitary channel conductance was determined to be 80 pS. This ion channel (LEAC, for large conductance elicitor-activated ion channel) is reversibly activated upon treatment of parsley protoplasts with an oligopeptide elicitor derived from a cell wall protein of Phytophthora sojae. Structural features of the elicitor found previously to be essential for receptor binding, induction of defense-related gene expression, and phytoalexin formation are identical to those required for activation of LEAC. Thus, receptor-mediated stimulation of this channel appears to be causally involved in the signaling cascade triggering pathogen defense in parsley.
  • Die Leibniz-Gemeinschaft
  • Digitalisierung in der Landwirtschaft
  • Martin-Luther Universität Halle
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