Publications - Stress and Develop Biology
Search narrowed by
Advanced Search
- Type of publication
- Publication (15)
- Books and chapters (3)
- Year
- Journal / Volume / Preprint Server Sorted by frequency and by alphabetical order
- Trends Plant Sci. (3)
- 0 (2)
- Phytochemistry (2)
- BBA-Mol. Cell Biol. Lipids (1)
- Crit. Rev. Plant Sci. (1)
- EMBO J. (1)
- Eur. J. Plant Pathol. (1)
- J. Biol. Chem. (1)
- Mol. Plant Microbe Interact. (1)
- Physiol. Mol. Plant Pathol. (1)
- Plant Cell Physiol. (1)
- Plant J. (1)
- Planta (1)
- The Mycota (1)
- Author Sorted by frequency and by alphabetical order
- Scheel, D. (9)
- Rosahl, S. (5)
- Clemens, S. (4)
- Knogge, W. (3)
- Lee, J. (3)
- Nürnberger, T. (3)
- Brunner, F. (2)
- Feussner, I. (2)
- Göbel, C. (2)
- Nies, D. H. (2)
- Rudd, J. J. (2)
- Baumert, A. (1)
- Block, A. (1)
- Bloss, T. (1)
- Bloß, T. (1)
- Champion, A. (1)
- Dangl, J. L. (1)
- Darvill, A. G. (1)
- Degenkolb, T. (1)
- Ecker, J. R. (1)
- Ellis, B. E. (1)
- Fiegen, M. (1)
- Geiler, C. (1)
- Govers, F. (1)
- Hahlbrock, K. (1)
- Hamberg, M. (1)
- Heberle-Bors, E. (1)
- Henry, Y. (1)
- Hirt, H. (1)
- Hunger, A. (1)
- Ichimura, K. (1)
- Innes, R. W. (1)
- Kauppinen, S. (1)
- Klessig, D. F. (1)
- Kreis, M. (1)
- Krämer, U. (1)
- Landgraf, P. (1)
- Landtag, J. (1)
- Lois, R. (1)
- Lozoya, E. (1)
- Machida, Y. (1)
- Morris, P. C. (1)
- Mundy, J. (1)
- Nass, N. (1)
- Neumann, D. (1)
- Ohashi, Y. (1)
- Palmgren, M. G. (1)
- Parker, J. (1)
- Petters, J. (1)
- Rasmussen, G. (1)
- Rose, J. K. C. (1)
- Schmidt, J. (1)
- Schroeder, J. I. (1)
- Sheen, J. (1)
- Shinozaki, K. (1)
- Strack, D. (1)
- Tena, G. (1)
- Thomine, S. (1)
- Tornero, P. (1)
- Varet, A. (1)
- Vess, C. (1)
- Walker, J. C. (1)
- Wilson, C. (1)
- Wirtz, W. (1)
- Wray, V. (1)
- Zhang, S. (1)
- van't Slot, K. A. E. (1)
- zur Nieden, U. (1)
Displaying results 1 to 10 of 18.
- 1
- 2
Landtag, J.; Baumert, A.; Degenkolb, T.; Schmidt, J.; Wray, V.; Scheel, D.; Strack, D.; Rosahl, S.; Accumulation of tyrosol glucoside in transgenic potato plants expressing a parsley tyrosine decarboxylase Phytochemistry 60, 683-689, (2002) DOI: 10.1016/S0031-9422(02)00161-9
As part of the response to pathogen infection, potato plants accumulate soluble and cell wall-bound phenolics such as hydroxycinnamic acid tyramine amides. Since incorporation of these compounds into the cell wall leads to a fortified barrier against pathogens, raising the amounts of hydroxycinnamic acid tyramine amides might positively affect the resistance response. To this end, we set out to increase the amount of tyramine, one of the substrates of the hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)-transferase reaction, by placing a cDNA encoding a pathogen-induced tyrosine decarboxylase from parsley under the control of the 35S promoter and introducing the construct into potato plants via Agrobacterium tumefaciens-mediated transformation. While no alterations were observed in the pattern and quantity of cell wall-bound phenolic compounds in transgenic plants, the soluble fraction contained several new compounds. The major one was isolated and identified as tyrosol glucoside by liquid chromatography–electrospray ionization–high resolution mass spectrometry and NMR analyses. Our results indicate that expression of a tyrosine decarboxylase in potato does not channel tyramine into the hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)-transferase reaction but rather unexpectedly, into a different pathway leading to the formation of a potential storage compound.Expression of a parsley tyrosine decarboxylase in potato unexpectedly channels tyramine into a pathway leading to the formation of tyrosol glucoside.
Landgraf, P.; Feussner, I.; Hunger, A.; Scheel, D.; Rosahl, S.; Systemic Accumulation of 12-oxo-phytodienoic Acid in SAR-induced Potato Plants Eur. J. Plant Pathol. 108, 279-283, (2002) DOI: 10.1023/A:1015132615650
In potato plants induced for systemic resistance by infiltration with Pseudomonas syringae pv. maculicola, 12-oxo-phytodienoic acid (OPDA) accumulated in infiltrated leaves as well as in non-treated leaves of infected plants. In contrast, jasmonic acid (JA) levels increased only in infiltrated leaves, suggesting that the biosynthetic precursor of JA, OPDA, might play a role in systemic acquired resistance.
Ichimura, K.; Shinozaki, K.; Tena, G.; Sheen, J.; Henry, Y.; Champion, A.; Kreis, M.; Zhang, S.; Hirt, H.; Wilson, C.; Heberle-Bors, E.; Ellis, B. E.; Morris, P. C.; Innes, R. W.; Ecker, J. R.; Scheel, D.; Klessig, D. F.; Machida, Y.; Mundy, J.; Ohashi, Y.; Walker, J. C.; Mitogen-activated protein kinase cascades in plants: a new nomenclature Trends Plant Sci. 7, 301-308, (2002) DOI: 10.1016/S1360-1385(02)02302-6
Mitogen-activated protein kinase (MAPK) cascades are universal signal transduction modules in eukaryotes, including yeasts, animals and plants. These protein phosphorylation cascades link extracellular stimuli to a wide range of cellular responses. In plants, MAPK cascades are involved in responses to various biotic and abiotic stresses, hormones, cell division and developmental processes. Completion of the Arabidopsis genome-sequencing project has revealed the existence of 20 MAPKs, 10 MAPK kinases and 60 MAPK kinase kinases. Here, we propose a simplified nomenclature for Arabidopsis MAPKs and MAPK kinases that might also serve as a basis for standard annotation of these gene families in all plants.
Göbel, C.; Feussner, I.; Hamberg, M.; Rosahl, S.; Oxylipin profiling in pathogen-infected potato leaves BBA-Mol. Cell Biol. Lipids 1584, 55-64, (2002) DOI: 10.1016/S1388-1981(02)00268-8
Plants respond to pathogen attack with a multicomponent defense response. Synthesis of oxylipins via the lipoxygenase (LOX) pathway appears to be an important factor for establishment of resistance in a number of pathosystems. In potato cells, pathogen-derived elicitors preferentially stimulate the 9-LOX-dependent metabolism of polyunsaturated fatty acids (PUFAs). Here we show by oxylipin profiling that potato plants react to pathogen infection with increases in the amounts of the 9-LOX-derived 9,10,11- and 9,12,13-trihydroxy derivatives of linolenic acid (LnA), the divinyl ethers colnelenic acid (CnA) and colneleic acid (CA) as well as 9-hydroxy linolenic acid. Accumulation of these compounds is faster and more pronounced during the interaction of potato with the phytopathogenic bacterium Pseudomonas syringae pv. maculicola, which does not lead to disease, compared to the infection of potato with Phytophthora infestans, the causal agent of late blight disease. Jasmonic acid (JA), a 13-LOX-derived oxylipin, accumulates in potato leaves after infiltration with P. syringae pv. maculicola, but not after infection with P. infestans.
Fiegen, M.; Knogge, W.; Amino acid alterations in isoforms of the effector protein NIP1 from Rhynchosporium secalis have similar effects on its avirulence- and virulence-associated activities on barley Physiol. Mol. Plant Pathol. 61, 299-302, (2002) DOI: 10.1006/pmpp.2002.0442
The secreted effector protein NIP1 from the barley pathogen Rhynchosporium secalis is a specific elicitor of defense reactions in host plants carrying the resistance gene Rrs1. In addition, it has activities associated with fungal virulence; independent of the plant genotype it stimulates the plant plasma membrane H+-ATPase and induces leaf necrosis. Four NIP1 isoforms differing in single amino acid residues were isolated from various naturally occurring fungal strains. All three activities of the protein (race specificity, H+-ATPase stimulation, necrosis induction) were affected by the amino acid alterations in a similar way suggesting that they are mediated through a single plant receptor.
Clemens, S.; Bloss, T.; Vess, C.; Neumann, D.; Nies, D. H.; zur Nieden, U.; A Transporter in the Endoplasmic Reticulum of Schizosaccharomyces pombe Cells Mediates Zinc Storage and Differentially Affects Transition Metal Tolerance J. Biol. Chem. 277, 18215-18221, (2002) DOI: 10.1074/jbc.M201031200
The cation diffusion facilitator (CDF) family represents a class of ubiquitous metal transporters. Inactivation of a CDF in Schizosaccharomyces pombe, Zhf, causes drastically different effects on the tolerance toward various metals. A deletion mutant is Zn2+/Co2+-hypersensitive yet displays significantly enhanced Cd2+ and Ni2+ tolerance. Accumulation of zinc, cobalt, and cadmium is reduced in mutant cells. Non-vacuolar zinc content, as measured by analytical electron microscopy, is lower in zhf− cells compared with wild-type cells in the presence of elevated Zn2+concentrations. The protective effect against cadmium toxicity is independent of the phytochelatin detoxification pathway. Phytochelatin synthase-deficient cells show extremely enhanced (about 200-fold) cadmium tolerance when zhf is disrupted. Immunogold labeling indicates endoplasmic reticulum (ER) localization of Zhf. Electron spectroscopic imaging shows that accumulation of zinc coincides with Zhf localization, demonstrating a major role of the ER for metal storage and the involvement of Zhf in cellular zinc homeostasis. Also, these observations indicate that Cd2+ions exert their toxic effects on cellular metabolism in the ER rather than in the cytosol.
Clemens, S.; Palmgren, M. G.; Krämer, U.; A long way ahead: understanding and engineering plant metal accumulation Trends Plant Sci. 7, 309-315, (2002) DOI: 10.1016/S1360-1385(02)02295-1
Some plants can hyperaccumulate metal ions that are toxic to virtually all other organisms at low dosages. This trait could be used to clean up metal-contaminated soils. Moreover, the accumulation of heavy metals by plants determines both the micronutrient content and the toxic metal content of our food. Complex interactions of transport and chelating activities control the rates of metal uptake and storage. In recent years, several key steps have been identified at the molecular level, enabling us to initiate transgenic approaches to engineer the transition metal content of plants.
Brunner, F.; Rosahl, S.; Lee, J.; Rudd, J. J.; Geiler, C.; Kauppinen, S.; Rasmussen, G.; Scheel, D.; Nürnberger, T.; Pep-13, a plant defense-inducing pathogen-associated pattern from Phytophthora transglutaminases EMBO J. 21, 6681-6688, (2002) DOI: 10.1093/emboj/cdf667
Innate immunity, an ancient form of defense against microbial infection, is well described for animals and is also suggested to be important for plants. Discrimination from self is achieved through receptors that recognize pathogen‐associated molecular patterns (PAMPs) not found in the host. PAMPs are evolutionarily conserved structures which are functionally important and, thus, not subject to frequent mutation. Here we report that the previously described peptide elicitor of defense responses in parsley, Pep‐13, constitutes a surface‐exposed fragment within a novel calcium‐dependent cell wall transglutaminase (TGase) from Phytophthora sojae . TGase transcripts and TGase activity are detectable in all Phytophthora species analyzed, among which are some of the most destructive plant pathogens. Mutational analysis within Pep‐13 identified the same amino acids indispensable for both TGase and defense‐eliciting activity. Pep‐13, conserved among Phytophthora TGases, activates defense in parsley and potato, suggesting its function as a genus‐specific recognition determinant for the activation of plant defense in host and non‐host plants. In summary, plants may recognize PAMPs with characteristics resembling those known to trigger innate immune responses in animals.
Brunner, F.; Wirtz, W.; Rose, J. K. C.; Darvill, A. G.; Govers, F.; Scheel, D.; Nürnberger, T.; A β-glucosidase/xylosidase from the phytopathogenic oomycete, Phytophthora infestans Phytochemistry 59, 689-696, (2002) DOI: 10.1016/S0031-9422(02)00045-6
An 85-kDa β-glucosidase/xylosidase (BGX1) was purified from the axenically grown phytopathogenic oomycete, Phytophthora infestans. The bgx1 gene encodes a predicted 61-kDa protein product which, upon removal of a 21 amino acid leader peptide, accumulates in the apoplastic space. Extensive N-mannosylation accounts for part of the observed molecular mass difference. BGX1 belongs to family 30 of the glycoside hydrolases and is the first such oomycete enzyme deposited in public databases. The bgx1 gene was found in various Phytophthora species, but is apparently absent in species of the related genus, Pythium. Despite significant sequence similarity to human and murine lysosomal glucosylceramidases, BGX1 demonstrated neither glucocerebroside nor galactocerebroside-hydrolyzing activity. The native enzyme exhibited glucohydrolytic activity towards 4-methylumbelliferyl (4-MU) β-d-glucopyranoside and, to lesser extent, towards 4-MU-d-xylopyranoside, but not towards 4-MU-β-d-glucopyranoside. BGX1 did not hydrolyze carboxymethyl cellulose, cellotetraose, chitosan or xylan, suggesting high substrate specificity and/or specific cofactor requirements for enzymatic activity.A β-glucosidase/xylosidase was purified from the phytopathogenic oomycete, Phytophthora infestans. The encoding gene is the first such sequence reported from a species of the kingdom chromista.
Bloß, T.; Clemens, S.; Nies, D. H.; Characterization of the ZAT1p zinc transporter from Arabidopsis thaliana in microbial model organisms and reconstituted proteoliposomes Planta 214, 783-791, (2002) DOI: 10.1007/s00425-001-0677-1
The ZAT1p zinc transporter from Arabidopsis thaliana (L.) Heynh. is a member of the cation diffusion facilitator (CDF) protein family. When heterologously expressed in Escherichia coli, ZAT1p bound zinc in a metal blot. Binding of zinc occurred mainly to the hydrophilic amino acid region from H182 to H232. A ZAT1p/ZAT1p*Δ(M1–I25) protein mixture was purified and reconstituted into proteoliposomes. Uptake of zinc into the proteoliposomes did not require a proton gradient across the liposomal membrane. ZAT1p did not transport cobalt, and transported cadmium at only 1% of the zinc transport rate. ZAT1p functioned as an uptake system for 65Zn2+ in two strains of the Gram-negative bacterium Ralstonia metallidurans, which were different in their content of zinc-efflux systems. The ZAT1 gene did not rescue increased zinc sensitivity of a ΔZRC1 single-mutant strain or of a ΔZRC1 ΔCOT1 double-mutant strain of Saccharomyces cerevisiae, but ZAT1 complemented this phenotype in a ΔSpZRC1 mutant strain of Schizosaccharomyces pombe.
- 1
- 2
