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Publikationen - Molekulare Signalverarbeitung

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Publikation

Kienow, L.; Schneider, K.; Bartsch, M.; Stuible, H.-P.; Weng, H.; Miersch, O.; Wasternack, C.; Kombrink, E.; Jasmonates meet fatty acids: functional analysis of a new acyl-coenzyme A synthetase family from Arabidopsis thaliana J. Exp. Bot. 59, 403-419, (2008) DOI: 10.1093/jxb/erm325

Arabidopsis thaliana contains a large number of genes encoding carboxylic acid-activating enzymes, including long-chain fatty acyl-CoA synthetase (LACS), 4-coumarate:CoA ligases (4CL), and proteins closely related to 4CLs with unknown activities. The function of these 4CL-like proteins was systematically explored by applying an extensive substrate screen, and it was uncovered that activation of fatty acids is the common feature of all active members of this protein family, thereby defining a new group of fatty acyl-CoA synthetase, which is distinct from the known LACS family. Significantly, four family members also displayed activity towards different biosynthetic precursors of jasmonic acid (JA), including 12-oxo-phytodienoic acid (OPDA), dinor-OPDA, 3-oxo-2(2′-[Z]-pentenyl)cyclopentane-1-octanoic acid (OPC-8), and OPC-6. Detailed analysis of in vitro properties uncovered significant differences in substrate specificity for individual enzymes, but only one protein (At1g20510) showed OPC-8:CoA ligase activity. Its in vivo function was analysed by transcript and jasmonate profiling of Arabidopsis insertion mutants for the gene. OPC-8:CoA ligase expression was activated in response to wounding or infection in the wild type but was undetectable in the mutants, which also exhibited OPC-8 accumulation and reduced levels of JA. In addition, the developmental, tissue- and cell-type specific expression pattern of the gene, and regulatory properties of its promoter were monitored by analysing promoter::GUS reporter lines. Collectively, the results demonstrate that OPC-8:CoA ligase catalyses an essential step in JA biosynthesis by initiating the β-oxidative chain shortening of the carboxylic acid side chain of its precursors, and, in accordance with this function, the protein is localized in peroxisomes.
Publikation

Brüx, A.; Liu, T.-Y.; Krebs, M.; Stierhof, Y.-D.; Lohmann, J. U.; Miersch, O.; Wasternack, C.; Schumacher, K.; Reduced V-ATPase Activity in the trans-Golgi Network Causes Oxylipin-Dependent Hypocotyl Growth Inhibition in Arabidopsis Plant Cell 20, 1088-1100, (2008) DOI: 10.1105/tpc.108.058362

Regulated cell expansion allows plants to adapt their morphogenesis to prevailing environmental conditions. Cell expansion is driven by turgor pressure created by osmotic water uptake and is restricted by the extensibility of the cell wall, which in turn is regulated by the synthesis, incorporation, and cross-linking of new cell wall components. The vacuolar H+-ATPase (V-ATPase) could provide a way to coordinately regulate turgor pressure and cell wall synthesis, as it energizes the secondary active transport of solutes across the tonoplast and also has an important function in the trans-Golgi network (TGN), which affects synthesis and trafficking of cell wall components. We have previously shown that det3, a mutant with reduced V-ATPase activity, has a severe defect in cell expansion. However, it was not clear if this is caused by a defect in turgor pressure or in cell wall synthesis. Here, we show that inhibition of the tonoplast-localized V-ATPase subunit isoform VHA-a3 does not impair cell expansion. By contrast, inhibition of the TGN-localized isoform VHA-a1 is sufficient to restrict cell expansion. Furthermore, we provide evidence that the reduced hypocotyl cell expansion in det3 is conditional and due to active, hormone-mediated growth inhibition caused by a cell wall defect.
Publikation

Stenzel, I.; Hause, B.; Proels, R.; Miersch, O.; Oka, M.; Roitsch, T.; Wasternack, C.; The AOC promoter of tomato is regulated by developmental and environmental stimuli Phytochemistry 69, 1859-1869, (2008) DOI: 10.1016/j.phytochem.2008.03.007

The allene oxide cyclase (AOC) catalyzes the formation of cis-(+)-12-oxophytodienoic acid, an intermediate in jasmonate biosynthesis and is encoded by a single copy gene in tomato. The full length AOC promoter isolated by genome walk contains 3600 bp. Transgenic tomato lines carrying a 1000 bp promoter fragment and the full length promoter, respectively, in front of the β-glucuronidase (GUS)-encoding uidA gene and several tobacco lines carrying the full length tomato AOC promoter before GUS were used to record organ- and tissue-specific promoter activities during development and in response to various stimuli. High promoter activities corresponding to immunocytochemically detected occurrence of the AOC protein were found in seeds and young seedlings and were confined to the root tip, hypocotyl and cotyledons of 3-d-old seedlings. In 10-d-old seedlings promoter activity appeared preferentially in the elongation zone. Fully developed tomato leaves were free of AOC promoter activity, but showed high activity upon wounding locally and systemically or upon treatment with JA, systemin or glucose. Tomato flowers showed high AOC promoter activities in ovules, sepals, anthers and pollen. Most of the promoter activity patterns found in tomato with the 1000 bp promoter fragment were also detected with the full length tomato AOC promoter in tobacco during development or in response to various stimuli. The data support a spatial and temporal regulation of JA biosynthesis during development and in response to environmental stimuli.
Publikation

Schilling, S.; Wasternack, C.; Demuth, H.-U.; Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution Biol. Chem. 389, (2008) DOI: 10.1515/BC.2008.111

Several mammalian peptide hormones and proteins from plant and animal origin contain an N-terminal pyroglutamic acid (pGlu) residue. Frequently, the moiety is important in exerting biological function in either mediating interaction with receptors or stabilizing against N-terminal degradation. Glutaminyl cyclases (QCs) were isolated from different plants and animals catalyzing pGlu formation. The recent resolution of the 3D structures of Carica papaya and human QCs clearly supports different evolutionary origins of the proteins, which is also reflected by different enzymatic mechanisms. The broad substrate specificity is revealed by the heterogeneity of physiological substrates of plant and animal QCs, including cytokines, matrix proteins and pathogenesis-related proteins. Moreover, recent evidence also suggests human QC as a catalyst of pGlu formation at the N-terminus of amyloid peptides, which contribute to Alzheimer's disease. Obviously, owing to its biophysical properties, the function of pGlu in plant and animal proteins is very similar in terms of stabilizing or mediating protein and peptide structure. It is possible that the requirement for catalysis of pGlu formation under physiological conditions may have triggered separate evolution of QCs in plants and animals.
Publikation

Miersch, O.; Neumerkel, J.; Dippe, M.; Stenzel, I.; Wasternack, C.; Hydroxylated jasmonates are commonly occurring metabolites of jasmonic acid and contribute to a partial switch-off in jasmonate signaling New Phytol. 177, 114-127, (2008) DOI: 10.1111/j.1469-8137.2007.02252.x

In potato 12‐hydroxyjasmonic acid (12‐OH‐JA) is a tuber‐inducing compound. Here, it is demonstrated that 12‐OH‐JA, as well as its sulfated and glucosylated derivatives, are constituents of various organs of many plant species. All accumulate differentially and usually to much higher concentrations than jasmonic acid (JA).In wounded tomato leaves, 12‐OH‐JA and its sulfated, as well as glucosylated, derivative accumulate after JA, and their diminished accumulation in wounded leaves of the JA‐deficient mutants spr2 and acx1 and also a JA‐deficient 35S::AOCantisense line suggest their JA‐dependent formation.To elucidate how signaling properties of JA/JAME (jasmonic acid methyl ester) are affected by hydroxylation and sulfation, germination and root growth were recorded in the presence of the different jasmonates, indicating that 12‐OH‐JA and 12‐hydroxyjasmonic acid sulfate (12‐HSO4‐JA) were not bioactive. Expression analyses for 29 genes showed that expression of wound‐inducible genes such as those coding for PROTEINASE INHIBITOR2, POLYPHENOL OXIDASE, THREONINE DEAMINASE or ARGINASE was induced by JAME and less induced or even down‐regulated by 12‐OH‐JA and 12‐HSO4‐JA. Almost all genes coding for enzymes in JA biosynthesis were up‐regulated by JAME but down‐regulated by 12‐OH‐JA and 12‐HSO4‐JA.The data suggest that wound‐induced metabolic conversion of JA/JAME into 12‐OH‐JA alters expression pattern of genes including a switch off in JA signaling for a subset of genes.
Publikation

Wasternack, C.; Feussner, I.; Multifunctional Enzymes in Oxylipin Metabolism ChemBioChem 9, 2373-2375, (2008) DOI: 10.1002/cbic.200800582

For the first time a member of the CYP74 enzyme subfamily (9‐AOS) from tomato has been shown by chemical and analytical approaches to catalyze multiple reactions. These multifunctional properties of 9‐AOS from the oxylipin‐forming lipoxygenase (LOX) pathway raise several new questions on lipid‐derived signaling.
Publikation

Feussner, I.; Wasternack, C.; Lipoxygenase catalyzed oxygenation of lipids Fett/Lipid 100, 146-152, (1998) DOI: 10.1002/(SICI)1521-4133(19985)100:4/5<146::AID-LIPI146>3.0.CO;2-D

Lipoxygenases (LOXs) and other LOX pathway enzymes are potentially able to form a large set of compounds being of commercial interest. Among them are conjugated dienic acids, jasmonates, and volatile aldehydes. Additionally, fatty acid hydroperoxides, formed by LOX, can serve as precursors for further transformation by either enzymes of the so‐called LOX pathway or by chemical reactions. In the case of linoleic acid more than one hundred products generated from its LOX‐derived fatty acid hydroperoxides have been described. Many of these products exhibit biological activity, suggesting a significant biological function of LOXs. This will be described for two different 13‐LOXs. (I) In various oilseeds we found that specific 13‐LOXs are localized at the lipid body membrane. They are capable of oxygenating esterified polyenoic fatty acids, such as triacylglycerols and phospho‐lipids. In addition, they form with arachidonic acid as substrate preferentially either 8‐ or 11‐hydroperoxy eicosatetraenoic acid, which is a very unusual positional specificity for plant LOXs. (II) From barley leaves we isolated another linoleate 13‐LOX form, which is localized within chloroplasts and is induced by jasmonic acid methyl ester. It is suggested, that this LOX form is capable of oxygenating linolenic acid residues of galactolipids. Examples will be presented for barley leaves of oxygenated derivatives of linolenic acid and compounds resulting from the hydroperoxide lyase‐branch of the LOX pathway.
Publikation

Churin, J.; Hause, B.; Feussner, I.; Maucher, H. P.; Feussner, K.; Börner, T.; Wasternack, C.; Cloning and expression of a new cDNA from monocotyledonous plants coding for a diadenosine 5′,5′′′-P1,P4-tetraphosphate hydrolase from barley (Hordeum vulgare) FEBS Lett. 431, 481-485, (1998) DOI: 10.1016/S0014-5793(98)00819-9

From a cDNA library generated from mRNA of white leaf tissues of the ribosome‐deficient mutant ‘albostrians' of barley (Hordeum vulgare cv. Haisa) a cDNA was isolated carrying 54.2% identity to a recently published cDNA which codes for the diadenosine‐5′,5′′′‐P1,P4‐tetraphosphate (Ap4A) hydrolase of Lupinus angustifolius (Maksel et al. (1998) Biochem. J. 329, 313–319), and 69% identity to four partial peptide sequences of Ap4A hydrolase of tomato. Overexpression in Escherichia coli revealed a protein of about 19 kDa, which exhibited Ap4A hydrolase activity and cross‐reactivity with an antibody raised against a purified tomato Ap4A hydrolase (Feussner et al. (1996) Z. Naturforsch. 51c, 477–486). Expression studies showed an mRNA accumulation in all organs of a barley seedling. Possible functions of Ap4A hydrolase in plants will be discussed.
Publikation

Bohlmann, H.; Vignutelli, A.; Hilpert, B.; Miersch, O.; Wasternack, C.; Apel, K.; Wounding and chemicals induce expression of the Arabidopsis thaliana gene Thi2.1, encoding a fungal defense thionin, via the octadecanoid pathway FEBS Lett. 437, 281-286, (1998) DOI: 10.1016/S0014-5793(98)01251-4

In seedlings of Arabidopsis thaliana the thionin gene Thi2.1 is inducible by methyl jasmonate, wounding, silver nitrate, coronatine, and sorbitol. We have used a biochemical and genetic approach to test the signal transduction of these different inducers. Both exogenously applied jasmonates and jasmonates produced endogenously upon stress induction, lead to GUS expression in a Thi2.1 promoter-uidA transgenic line. No GUS expression was observed in a coi1 mutant background which lacks jasmonate perception whereas methyl jasmonate and coronatine but not the other inducers were able to overcome the block in jasmonic acid production in a fad3-2 fad7-2 fad8 mutant background. Our results show conclusively that all these inducers regulate Thi2-1 gene expression via the octadecanoid pathway.
Publikation

Wasternack, C.; Miersch, O.; Kramell, R.; Hause, B.; Ward, J.; Beale, M.; Boland, W.; Parthier, B.; Feussner, I.; Jasmonic acid: biosynthesis, signal transduction, gene expression Fett/Lipid 100, 139-146, (1998) DOI: 10.1002/(SICI)1521-4133(19985)100:4/5<139::AID-LIPI139>3.0.CO;2-5

Jasmonic acid (JA) is an ubiquitously occurring plant growth regulator which functions as a signal of developmentally or environmentally regulated expression of various genes thereby contributing to the defense status of plants [1–5]. The formation of jasmonates in a lipid‐based signalling pathway via octadecanoids seems to be a common principle for many plant species to express wound‐ and stressinduced genes [4, 5].There are various octadecanoid‐derived signals [3]. Among them, jasmonic acid and its amino acid conjugates are most active in barley, supporting arguments that β‐oxidation is an essential step in lipid‐based JA mediated responses. Furthermore, among derivatives of 12‐oxophytodienoic acid (PDA) carrying varying length of the carboxylic acid side‐chain, only those with a straight number of carbon atoms are able to induce JA responsive genes in barley leaves after treatment with these compounds. Barley leaves stressed by treatment with sorbitol solutions exhibit mainly an endogenous rise of JA and JA amino acid conjugates suggesting that both of them are stress signals. Data on organ‐ and tissue‐specific JA‐responsive gene expression will be presented and discussed in terms of “JA as a master switch” among various lipid‐derived signals.
  • Die Leibniz-Gemeinschaft
  • Digitalisierung in der Landwirtschaft
  • Martin-Luther Universität Halle
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