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Publikationen - Molekulare Signalverarbeitung

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Bücher und Buchkapitel

Wasternack, C. & Hause, B. Benno Parthier und die Jasmonatforschung in Halle Nova Acta Leopoldina, NF Supplementum 28, 29-38, (2013) ISBN: ISBN 978-3-8047-3209-4

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Bücher und Buchkapitel

Ziegler, J.; Hamberg, M.; Miersch, O. Allene oxide cyclase from corn: Partial purification and characterization (Williams, J.P., Mobashsher, U., Khan, M.U., Lem, N.W.). Kluwer Academic Publishers, Dordrecht 99-101, (1997)

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Bücher und Buchkapitel

Feussner, I.; Kühn, H.; Wasternack, C. Do Lipoxygenases initiate ß-oxidation? (Williams, J.P., Mobashsher, U., Khan, M.U. & Lem, N.W.). Kluwer Academic Publishers, Dordrecht 250-252, (1997)

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Publikation

Wasternack, C.; Hause, B. Jasmonates: biosynthesis, perception, signal transduction and action in plant stress response, growth and development. An update to the 2007 review in <span>Annals of Botany</span> Annals of Botany 111, 1021-1058, (2013) DOI: 10.1093/aob/mct067

Background: Jasmonates are important regulators in plant responses to biotic and abiotic stresses as well as indevelopment. Synthesized from lipid-constituents, the initially formed jasmonic acid is converted to differentmetabolites including the conjugate with isoleucine. Important new components of jasmonate signalling includingits receptor were identified, providing deeper insight into the role of jasmonate signalling pathways in stressresponses and development.Scope: The present review is an update of the review on jasmonates published in this journal in 2007. New dataof the last five years are described with emphasis on metabolites of jasmonates, on jasmonate perception andsignalling, on cross-talk to other plant hormones and on jasmonate signalling in response to herbivores and pathogens,in symbiotic interactions, in flower development, in root growth and in light perception.Conclusions: The last few years have seen breakthroughs in the identification of JASMONATE ZIM DOMAIN(JAZ) proteins and their interactors such as transcription factors and co-repressors, and the crystallization of thejasmonate receptor as well as of the enzyme conjugating jasmonate to amino acids. Now, the complex nature ofnetworks of jasmonate signalling in stress responses and development including hormone cross-talk can beaddressed.
Publikation

Kopycki, J.; Wieduwild, E.; Kohlschmidt, J.; Brandt, W.; Stepanova, A.N.; Alonso, J.M.; Pedras, M.S.; Abel, S.; Grubb, C.D. Kinetic analysis of Arabidopsis glucosyltransferase UGT74B1 illustrates a general mechanism by which enzymes can escape product inhibition Biochem J 450, 37-46, (2013) DOI: 10.1042/BJ20121403

Plant genomes encode numerous small molecule glycosyltransferases which modulate the solubility, activity, immunogenicity and/or reactivity of hormones, xenobiotics and natural products. The products of these enzymes can accumulate to very high concentrations, yet somehow avoid inhibiting their own biosynthesis. Glucosyltransferase UGT74B1 (UDP-glycosyltransferase 74B1) catalyses the penultimate step in the core biosynthetic pathway of glucosinolates, a group of natural products with important functions in plant defence against pests and pathogens. We found that mutation of the highly conserved Ser284 to leucine [wei9-1 (weak ethylene insensitive)] caused only very mild morphological and metabolic phenotypes, in dramatic contrast with knockout mutants, indicating that steady state glucosinolate levels are actively regulated even in unchallenged plants. Analysis of the effects of the mutation via a structural modelling approach indicated that the affected serine interacts directly with UDP-glucose, but also predicted alterations in acceptor substrate affinity and the kcat value, sparking an interest in the kinetic behaviour of the wild-type enzyme. Initial velocity and inhibition studies revealed that UGT74B1 is not inhibited by its glycoside product. Together with the effects of the missense mutation, these findings are most consistent with a partial rapid equilibrium ordered mechanism. This model explains the lack of product inhibition observed both in vitro and in vivo, illustrating a general mechanism whereby enzymes can continue to function even at very high product/precursor ratios.
Publikation

Hause, B.; Kogel, K.-H.; Parthier, B.; Wasternack, C. In barley leaf cells, jasmonates do not act as a signal during compatible or incompatible interactions with the powdery mildew fungus (<i>Erysiphe graminis</i> f. sp. <i>hordei</i>) J. Plant Physiol. 150, 127-132, (1997) DOI: 10.1016/S0176-1617(97)80191-5

We have studied a possible function of jasmonates as mediators in the host-pathogen interaction of barley (Hordeum vulgare L.) with the powdery mildew fungus Egh (Erysiphe graminis f. sp. hordei). Previous findings from whole-leaf extracts demonstrated that (i) extracts from infected barley leaves did not contain enhanced levels of jasmonates, (ii) transcripts of jasmonate-inducible genes were not expressed upon infection, and (iii) exogenous application of jasmonates did not induce resistance to Egh (Kogel et al., 1995). Nevertheless, the question arises whether or not jasmonates are involved in the interaction of barley with the powdery mildew fungus at the local site of infection. Using an immunocytological approach the analysis of leaf cross-sections from a susceptible barley cultivar and its near-isogenic mlo5-resistant line revealed no accumulation of JIP-23, the most abundant jasmonate inducible protein, neither in epidermal cells attacked by the pathogen nor in adjacent mesophyll cells. As a positive control, cross-sections from methyl jasmonate-treated leaf segments showed a strong signal for JIP-23 accumulation. Because the presence of the jasmonate-inducible protein is highly indicative for an already low threshold level of endogenous jasmonate (Lehmann et al., 1995), the lack of JIP-23 accumulation at the sites of attempted fungal infection clearly demonstrates the absence of enhanced levels of jasmonates. This excludes even a local rise of jasmonate confined to those single cells penetrated (Mlo genotype) or attacked (mlo5 genotype) by the fungus.
Publikation

Görschen, E.; Dunaeva, M.; Hause, B.; Reeh, I.; Wasternack, C.; Parthier, B. Expression of the ribosome-inactivating protein JIP60 from barley in transgenic tobacco leads to an abnormal phenotype and alterations on the level of translation Planta 202, 470-478, (1997)

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Publikation

Feussner, I.; Fritz, I.G.; Hause, B.; Ullrich, W.R.; Wasternack, C. Induction of a new lipoxygenase form in cucumber leaves by salicylic acid or 2,6-dichloroisonicotinic acid Bot. Acta 110, 101-108, (1997) DOI: 10.1111/j.1438-8677.1997.tb00616.x

Changes in lipoxygenase (LOX) protein pattern and/or activity were investigated in relation to acquired resistance of cucumber (Cucumis sativus L.) leaves against two powdery mildews, Sphaerotheca fuliginea (Schlecht) Salmon and Erysiphe cichoracearum DC et Merat. Acquired resistance was established by spraying leaves with salicylic acid (SA) or 2,6-dichloroisonicotinic acid (INA) and estimated in whole plants by infested leaf area compared to control plants. SA was more effective than INA. According to Western blots, untreated cucumber leaves contained a 97 kDa LOX form, which remained unchanged for up to 48 h after pathogen inoculation. Upon treatment with SA alone for 24 h or with INA plus pathogen, an additional 95 kDa LOX form appeared which had an isoelectric point in the alkaline range. For the induction of this form, a threshold concentration of 1 mM SA was required, higher SA concentrations did not change LOX-95 expression which remained similar between 24 h and 96 h but further increased upon mildew inoculation. Phloem exudates contained only the LOX-97 form, in intercellular washing fluid no LOX was detected. dichloroisonicotinic localization revealed LOX protein in the cytosol of the mesophyll cells without differences between the forms.
Publikation

Feussner, I.; Balkenhohl, T.J.; Porzel, A.; Kühn, H.; Wasternack, C. Structural elucidation of oxygenated storage lipids in cucumber cotyledons. Implication of lipid body lipoxygenase in lipid mobilization during germination J. Biol. Chem. 272, 21635-21641, (1997)

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Publikation

Feussner, I.; Porzel, A.; Wasternack, C.; Kühn, H. Quantitative Analyse von Lipoxygenase-Metaboliten in Lipiden durch NMR-Spektroskopie Biospektrum 3, 54-58, (1997)

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