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Publikationen - Molekulare Signalverarbeitung

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Bücher und Buchkapitel

Stumpe, M.; Stenzel, I.; Weichert, H.; Hause, B.; Feussner, I. The lipoxygenase pathway in mycorrhizal roots of <span>Medicago truncatula</span> (Murata, N., Yamada, M., Nishida, I., Okuyama, H., Sekijar, J., Hajme, W.). Kluwer Academic Publishers, Dordrecht 287-290, (2003)

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Bücher und Buchkapitel

Stenzel, I.; Hause, B.; Feussner, I.; Wasternack, C. Transcriptional activation of jasmonate biosynthesis enzymes is not reflected at protein level (Murata, N., Yamada, M., Nishida, I., Okuyama, H., Sekijar, J., Hajme, W.). Kluwer Academic Publishers 267-270, (2003)

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Publikation

Gidda, K.S.; Miersch, O.; Schmidt, J.; Wasternack, C.; Varin, L. Biochemical and molecular characterization of a hydroxy-jasmonate sulfotransferase from Arabidopsis thaliana J. Biol. Chem. 278, 17895-17900, (2003) DOI: 10.1074/jbc.M211943200

12-Hydroxyjasmonate, also known as tuberonic acid, was first isolated from Solanum tuberosum and was shown to have tuber-inducing properties. It is derived from the ubiquitously occurring jasmonic acid, an important signaling molecule mediating diverse developmental processes and plant defense responses. We report here that the gene AtST2a from Arabidopsis thaliana encodes a hydroxyjasmonate sulfotransferase. The recombinant AtST2a protein was found to exhibit strict specificity for 11- and 12-hydroxyjasmonate with Km values of 50 and 10 µM, respectively. Furthermore, 12-hydroxyjasmonate and its sulfonated derivative are shown to be naturally occurring in A. thaliana. The exogenous application of methyljasmonate to A. thaliana plants led to increased levels of both metabolites, whereas treatment with 12-hydroxyjasmonate led to increased level of 12-hydroxyjasmonate sulfate without affecting the endogenous level of jasmonic acid. AtST2a expression was found to be induced following treatment with methyljasmonate and 12-hydroxyjasmonate. In contrast, the expression of the methyljasmonate-responsive gene Thi2.1, a marker gene in plant defense responses, is not induced upon treatment with 12-hydroxyjasmonate indicating the existence of independent signaling pathways responding to jasmonic acid and 12-hydroxyjasmonic acid. Taken together, the results suggest that the hydroxylation and sulfonation reactions might be components of a pathway that inactivates excess jasmonic acid in plants. Alternatively, the function of AtST2a might be to control the biological activity of 12-hydroxyjasmonic acid.
Publikation

O'Donnell, P.J.; Schmelz, E.; Block, A.; Miersch, O.; Wasternack, C.; Jones, J.B.; Klee, H.J. Multiple hormones cooperatively control a susceptible tomato pathogen defense response Plant Physiol. 133, 1181-1189, (2003)

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Publikation

Schilling, S.; Niestroj, A.J.; Rahfeld, J.-U.; Hoffmann, T.; Wermann, M.; Zunkel, K.; Wasternack, C.; Demuth, H.-U. Identification of human glutaminyl cyclase as a metalloenzyme - Potent inhibition by imidazole derivatives and heterocyclic chelators J. Biol. Chem. 278, 49773-49779, (2003)

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Publikation

Schilling, S.; Manhart, S.; Hoffmann, T.; Ludwig, H.-H.; Wasternack, C.; Demuth, H.-U. Substrate specificity of glutaminyl cyclases from plants and animals Biol. Chem. 384, 1583-1592, (2003)

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Bücher und Buchkapitel

Weichert, H.; Maucher, H.; Hornung, E.; Wasternack, C.; Feussner, I. Shift in fatty acid and oxylipin pattern of tomato leaves following overexpression of the allene oxide cyclase (Murata, N., Yamada, M., Nishida, I., Okuyama, H., Sekijar, J., Hajme, W.). Kluwer Academic Publishers 275-278, (2003)

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Publikation

Dingley, K.H.; Ubick, E.A.; Chiarappa-Zucca, M.L.; Nowell, S.; Abel, S.; Ebeler, S.E.; Mitchell, A.E.; Burns, S.A.; Steinberg, F.M.; Clifford, A.J. Effect of dietary constituents with chemopreventive potential on adduct formation of a low dose of the heterocyclic amines PhIP and IQ and Phase II hepatic enzymes Nutr & Cancer 46, 212 - 221, (2003)

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Publikation

Feussner, I.; Hause, B.; Nellen, A.; Wasternack, C.; Kindl, H. Lipid-body lipoxygenase is expressed in cotyledons during germination prior to other lipoxygenase forms Planta 198, 288-293, (1996) DOI: 10.1007/BF00206255

Lipid bodies are degraded during germination. Whereas some proteins, e.g. oleosins, are synthesized during the formation of lipid bodies of maturating seeds, a new set of proteins, including a specific form of lipoxygenase (LOX; EC 1.13.11.12), is detectable in lipid bodies during the stage of fat degradation in seed germination. In cotyledons of cucumber (Cucumis sativus L.) seedlings at day 4 of germination, the most conspicuous staining with anti-LOX antibodies was observed in the cytosol. At very early stages of germination, however, the LOX form present in large amounts and synthesized preferentially was the lipid-body LOX. This was demonstrated by immunocytochemical staining of cotyledons from 1-h and 24-h-old seedlings: the immunodecoration of sections of 24-h-old seedlings with anti-LOX antiserum showed label exclusively correlated with lipid bodies of around 3 μm in diameter. In accordance, the profile of LOX protein isolated from lipid bodies during various stages of germination showed a maximum at day 1. By measuring biosynthesis of the protein in vivo we demonstrated that the highest rates of synthesis of lipid-body LOX occurred at day 1 of germination. The early and selective appearance of a LOX form associated with lipid bodies at this stage of development is discussed.
Publikation

Herde, O.; Atzorn, R.; Fisahn, J.; Wasternack, C.; Willmitzer, L.; Peña-Cortés, H. Localized wounding by heat initiates the accumulation of proteinase inhibitor II in abscisic acid-deficient plants by triggering jasmonic acid biosynthesis Plant Physiol. 112, 853-860, (1996)

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