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Publications - Stress and Develop Biology

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Books and chapters

Clemens, S.; Simm, C.; Maier, T.; Heavy Metal‐binding Proteins and Peptides (2005) DOI: 10.1002/3527600035.bpol8010

IntroductionHistorical OutlineChemical StructuresNomenclature and Structure of MetallothioneinsPhytochelatins and Phytochelatin–Metal ComplexesStructural Properties of MetallochaperonesChemical Analysis and DetectionMetallothioneinsPhytochelatinsOccurrenceMetallothioneinsPhytochelatinsMetallochaperonesFunctionsMetal Homeostasis and the Role of MetallochaperonesBuffering and DetoxificationPhytochelatin FunctionsMetallothionein FunctionsPhysiologyMetallothionein Localization and IsoformsLocalization and Compartmentation of Phytochelatin SynthesisBiochemistryMetal‐binding Characteristics of MetallothioneinsBiochemistry of Phytochelatin SynthesisMolecular GeneticsMetallothionein Genes and Their RegulationPhytochelatin Synthase GenesBiotechnological ApplicationsPatentsOutlook and Perspectives
Books and chapters

Scheel, D.; Nuernberger, T.; Signal Transduction in Plant Defense Responses to Fungal Infection 1-30, (2004)

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Books and chapters

Rosahl, S.; Feussner, I.; Oxylipins 329-354, (2004)

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Books and chapters

Lee, J.; Nürnberger, T.; Is Pore Formation Activity of HrpZ Required for Defence Activation in Plant Cells? 165-173, (2003) DOI: 10.1007/978-94-017-0133-4_18

The HrpZ gene product, harpin, is an export substrate of the type III secretion system of phytopathogenic Pseudomonas syringae. The role of this protein in pathogenesis is largely unknown. We previously determined that HrpZ binds to lipids and can form cation pores in synthetic lipid bilayers. Such pore-forming activity may allow nutrient release during bacterial colonisation of host plants. In addition. HrpZ is known to trigger plant defence responses in a variety of plants, such as tobacco. We have previously also characterised a binding site in tobacco plasma membranes that likely mediates HrpZ-induced defence responses. In order to reconcile these findings, we pose the question as to whether the activation of plant defence responses by HrpZ is mediated through a “classical” receptor perception mode or if plant membrane perturbation through the inherent pore-forming activity of HrpZ may induce defence responses. As defence in parsley cells can be induced both in a receptor-mediated manner or through ionophores these cells served as an ideal system for our analysis. We first performed ligand binding studies to characterise the presence of a binding site/receptor. We further digested HrpZ with endopeptidases and used subfragments of HrpZ to assess the elicitor-active domain of HrpZ. A C-terminal region of HrpZ appears to be sufficient to elicit plant defence responses. A novel assay involving dye-loaded liposomes was developed to validate previous electrophysiological findings on HrpZ-mediated cation pore formation. More importantly, this assay was used to establish if the elicitor-active C-terminal fragment of HrpZ could form pores. Our findings suggest that the structural requirements for ion pore formation and activation of plant defence responses by HrpZ are different. Thus, ion pore formation alone may not explain the activation of plant defence by HrpZ.
Books and chapters

Scheel, D.; Oxidative burst and the role of reactive oxygen species in plant-pathogen interactions (Inzé, D. & van Montagu, M., eds.). 137-153, (2002)

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Books and chapters

Clemens, S.; Thomine, S.; Schroeder, J. I.; Molecular mechanisms that control plant tolerance to heavy metals and possible roles towards manipulating metal accumulation 665-691, (2002)

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Publications

Hornung, E.; Rosahl, S.; Kühn, H.; Feussner, I.; Creating lipoxygenases with new positional specificities by site-directed mutagenesis Biochem. Soc. Trans. 28, 825-826, (2000) DOI: 10.1042/bst0280825

In order to analyse the amino acid determinants which alter the positional specificity of plant lipoxygenases (LOXs), multiple LOX sequence alignments and structural modelling of the enzyme-substrate interactions were carried out. These alignments suggested three amino acid residues as the primary determinants of positional specificity. Here we show the generation of two plant LOXs with new positional specificities, a Δ-linoleneate 6-LOX and an arachidonate 11-LOX, by altering only one of these determinants within the active site of two plant LOXs. In the past, site-directed-mutagenesis studies have mainly been carried out with mammalian lipoxygenases (LOXs) [1]. In these experiments two regions have been identified in the primary structure containing sequence determinants for positional specificity. Amino acids aligning with the Sloane determinants [2] are highly conserved among plant LOXs. In contrast, there is amino acid hetero-geneity among plant LOXs at the position that aligns with P353 of the rabbit reticulocyte 15-LOX (Borngräber determinants) [3].
Publications

Noehringer, C.; Scheel, D.; Blée, E.; Lipoxygenase isoforms in elicitor-treated parsley cell suspension cultures Biochem. Soc. Trans. 28, 827-829, (2000) DOI: 10.1042/bst0280827

Treatment of parsley cell cultures with a fungal elicitor triggered the induction of a lipoxygenase isoform which may be involved in the de novo synthesis of defence-response inducers, such as jasmonic acid or 12-oxo-phytodienoic acid.
Books and chapters

Scheel, D.; Blume, B.; Brunner, F.; Fellbrich, G.; Dalbøge, H.; Hirt, H.; Kauppinen, S.; Kroj, T.; Ligterink, W.; Nürnberger, T.; Tschöpe, M.; Zinecker, H.; zur Nieden, U.; Receptor-mediated signal transduction in plant defense 131-135, (2000)

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Books and chapters

Bruns, I.; Sutter, K.; Neumann, D.; Krauss, G.-J.; Glutathione accumulation - a specific response of mosses to heavy metal stress 389-391, (2000)

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