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Publications - Stress and Develop Biology

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Publications

Barak, N. N.; Neumann, P.; Sevvana, M.; Schutkowski, M.; Naumann, K.; Malešević, M.; Reichardt, H.; Fischer, G.; Stubbs, M. T.; Ferrari, D. M.; Crystal Structure and Functional Analysis of the Protein Disulfide Isomerase-Related Protein ERp29 J. Mol. Biol. 385, 1630-1642, (2009) DOI: 10.1016/j.jmb.2008.11.052

The protein disulfide isomerase-related protein ERp29 is a putative chaperone involved in processing and secretion of secretory proteins. Until now, however, both the structure and the exact nature of interacting substrates remained unclear. We provide for the first time a crystal structure of human ERp29, refined to 2.9 Å, and show that the protein has considerable structural homology to its Drosophila homolog Wind. We show that ERp29 binds directly not only to thyroglobulin and thyroglobulin-derived peptides in vitro but also to the Wind client protein Pipe and Pipe-derived peptides, although it fails to process Pipe in vivo. A monomeric mutant of ERp29 and a D domain mutant in which the second peptide binding site is inactivated also bind protein substrates, indicating that the monomeric thioredoxin domain is sufficient for client protein binding. Indeed, the b domains of ERp29 or Wind, expressed alone, are sufficient for binding proteins and peptides. Interacting peptides have in common two or more aromatic residues, with stronger binding for sequences with overall basic character. Thus, the data allow a view of the two putative peptide binding sites of ERp29 and indicate that the apparent, different processing activity of the human and Drosophila proteins in vivo does not stem from differences in peptide binding properties.
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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Publications

Marković-Housley, Z.; Degano, M.; Lamba, D.; von Roepenack-Lahaye, E.; Clemens, S.; Susani, M.; Ferreira, F.; Scheiner, O.; Breiteneder, H.; Crystal Structure of a Hypoallergenic Isoform of the Major Birch Pollen Allergen Bet v 1 and its Likely Biological Function as a Plant Steroid Carrier J. Mol. Biol. 325, 123-133, (2003) DOI: 10.1016/S0022-2836(02)01197-X

Bet v 1l is a naturally occurring hypoallergenic isoform of the major birch pollen allergen Bet v 1. The Bet v 1 protein belongs to the ubiquitous family of pathogenesis-related plant proteins (PR-10), which are produced in defense-response to various pathogens. Although the allergenic properties of PR-10 proteins have been extensively studied, their biological function in plants is not known. The crystal structure of Bet v 1l in complex with deoxycholate has been determined to a resolution of 1.9 Å using the method of molecular replacement. The structure reveals a large hydrophobic Y-shaped cavity that spans the protein and is partly occupied by two deoxycholate molecules which are bound in tandem and only partially exposed to solvent. This finding indicates that the hydrophobic cavity may have a role in facilitating the transfer of apolar ligands. The structural similarity of deoxycholate and brassinosteroids (BRs) ubiquitous plant steroid hormones, prompted the mass spectrometry (MS) study in order to examine whether BRs can bind to Bet v 1l. The MS analysis of a mixture of Bet v 1l and BRs revealed a specific non-covalent interaction of Bet v 1l with brassinolide and 24-epicastasterone. Together, our findings are consistent with a general plant-steroid carrier function for Bet v 1 and related PR-10 proteins. The role of BRs transport in PR-10 proteins may be of crucial importance in the plant defense response to pathological situations as well as in growth and development.
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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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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