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Publications - Molecular Signal Processing

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Displaying results 21 to 30 of 33.

Publications

Feussner, I.; Wasternack, C. The lipoxygenase pathway Annu. Rev. Plant Biol. 53, 275-297, (2002)

Lipid peroxidation is common to all biological systems, both appearing in developmentally and environmentally regulated processes of plants. The hydroperoxy polyunsaturated fatty acids, synthesized by the action of various highly specialized forms of lipoxygenases, are substrates of at least seven different enzyme families. Signaling compounds such as jasmonates, antimicrobial and antifungal compounds such as leaf aldehydes or divinyl ethers, and a plant-specific blend of volatiles including leaf alcohols are among the numerous products. Cloning of many lipoxygenases and other key enzymes within the lipoxygenase pathway, as well as analyses by reverse genetic and metabolic profiling, revealed new reactions and the first hints of enzyme mechanisms, multiple functions, and regulation. These aspects are reviewed with respect to activation of this pathway as an initial step in the interaction of plants with pathogens, insects, or abiotic stress and at distinct stages of development.
Publications

Ellis, C.; Karafyllidis, I.; Wasternack, C.; Turner, J.G. The Arabidopsis mutant cev1 links cell wall signaling to jasmonate and ethylene responses The Plant Cell 14, 1557-1566, (2002)

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Publications

Abel, S.; Ticconi, C.A.; Delatorre, C.A. Phosphate sensing in higher plants Plant Physiology 115, 1 - 8, (2002)

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Publications

Weichert, H.; Kolbe, A.; Kraus, A.; Wasternack, C.; Feussner, I. Metabolic profiling of oxylipins in germinating cucumber seedlings - lipoxygenase-dependent degradation of triacylglycerols and biosynthesis of volatile aldehydes Planta 215, 612-619, (2002)

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Publications

Schwechheimer, C.; Calderón Villalobos, L.I. Cullin-containing E3 ubiquitin ligases in plant development Curr. Opin. Plant Biol. 7(6), 677-686, (2002)

In eukaryotes, the ubiquitinproteasome system participates in the control of signal transduction events by selectively eliminating regulatory proteins. E3 ubiquitin ligases specifically bind degradation substrates and mediate their poly-ubiquitylation, a prerequisite for their degradation by the 26S proteasome. On the basis of the analysis of the Arabidopsis genome sequence, it is predicted that there are more than 1000 E3 ubiquitin ligases in plants. Several types of E3 ubiquitin ligases have already been characterized in eukaryotes. Recently, some of these E3 enzymes have been implicated in specific plant signaling pathways.
Publications

Dussle, C.M.; Quint, M.; Xu, M.L.; Melchinger, A.E.; Lübberstedt, T. Conversion of AFLP fragments tightly linked to Scmv1 and Scmv2 into simple PCR-based markers Theor Appl Genet 105, 1190-1195, (2002)

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Publications

Laskowski, M.J.; Dreher, K.A.; Gehring, M.; Abel, S.; Gensler, A.; Sussex, I.M. FQR1, a novel primary auxin-response gene, encodes an FMN-binding quinone reductase. Plant Physiology 128, 578-686, (2002)

FQR1 is a novel primary auxin-response gene that codes for a flavin mononucleotide-binding flavodoxin-like quinone reductase. Accumulation of FQR1 mRNA begins within 10 min of indole-3-acetic acid application and reaches a maximum of approximately 10-fold induction 30 min after treatment. This increase in FQR1 mRNA abundance is not diminished by the protein synthesis inhibitor cycloheximide, demonstrating thatFQR1 is a primary auxin-response gene. Sequence analysis reveals that FQR1 belongs to a family of flavin mononucleotide-binding quinone reductases. Partially purified His-tagged FQR1 isolated fromEscherichia coli catalyzes the transfer of electrons from NADH and NADPH to several substrates and exhibits in vitro quinone reductase activity. Overexpression of FQR1 in plants leads to increased levels of FQR1 protein and quinone reductase activity, indicating that FQR1 functions as a quinone reductase in vivo. In mammalian systems, glutathione S-transferases and quinone reductases are classified as phase II detoxification enzymes. We hypothesize that the auxin-inducible glutathioneS-transferases and quinone reductases found in plants also act as detoxification enzymes, possibly to protect against auxin-induced oxidative stress.
Publications

Nibbe, M.; Hilpert, B.; Wasternack, C.; Miersch, O.; Apel, K. Cell death and salicylate- and jasmonate-dependent stress responses in Arabidopsis are controlled by single cet genes Planta 216, 120-128, (2002)

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Publications

Abdala, G.; Castro, G.; Miersch, O.; Pierce, D. Changes in jasmonate and gibberellin levels during development of potato plants (Solanum tuberosum) Plant Growth Reg. 36, 121-126, (2002)

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Publications

Schilling, S.; Hoffmann, T.; Wermann, M.; Heiser, U.; Wasternack, C.; Demuth, H.-U. Continuous spectrometric assays for glutaminyl cyclase activity Analytical Biochemistry 303, 49-56, (2002)

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