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Publikationen - Molekulare Signalverarbeitung

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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.

Bücher und Buchkapitel

Stumpe, M., Stenzel, I., Weichert, H., Hause, B. & Feussner, I. The lipoxygenase pathway in mycorrhizal roots of Medicago truncatula. In: Advanced Research on Plant Lipids (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. In: Advanced Research on Plant Lipids (Murata, N., Yamada, M., Nishida, I., Okuyama, H., Sekijar, J., Hajme, W.). Kluwer Academic Publishers 267-270, (2003)

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Publikation

de la Peña, M., Gago, S. & Flores, R. Peripheral regions of natural hammerhead ribozymes greatly increase their self-cleavage activity The EMBO Journal 22, 5561-5570, (2003)

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Publikation

Naum-Onganı́a, G., Gago-Zachert, S., Peña, E., Grau, O. & Garcia, M. L. Citrus psorosis virus RNA 1 is of negative polarity and potentially encodes in its complementary strand a 24K protein of unknown function and 280K putative RNA dependent RNA polymerase ☆ Virus Res 96, 49–61, (2003) DOI: 10.1016/S0168-1702(03)00172-2

Citrus psorosis virus (CPsV), the type member of genus Ophiovirus, has three genomic RNAs. Complete sequencing of CPsV RNA 1 revealed a size of 8184 nucleotides and Northern blot hybridization with chain specific probes showed that its non-coding strand is preferentially encapsidated. The complementary strand of RNA 1 contains two open reading frames (ORFs) separated by a 109-nt intergenic region, one located near the 5′-end potentially encoding a 24K protein of unknown function, and another of 280K containing the core polymerase motifs characteristic of viral RNA-dependent RNA polymerases (RdRp). Comparison of the core RdRp motifs of negative-stranded RNA viruses, supports grouping CPsV, Ranunculus white mottle virus (RWMV) and Mirafiori lettuce virus (MiLV) within the same genus (Ophiovirus), constituting a monophyletic group separated from all other negative-stranded RNA viruses. Furthermore, RNAs 1 of MiLV, CPsV and RWMV are similar in size and those of MiLV and CPsV also in genomic organization and sequence.

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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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. In: Advanced Research on Plant Lipids (Murata, N., Yamada, M., Nishida, I., Okuyama, H., Sekijar, J., Hajme, W.). Kluwer Academic Publishers 275-278, (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

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

Stenzel, I., Ziehte, K., Schurath, J., Hertel, S.C., Bosse, D. & Köck, M. Differential expression of PSI14, a phosphatase gene family, in response to phosphate availability, plant infection and pathogen infection Physiol. Plant 118, 138-146, (2003)

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