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Publikationen - Molekulare Signalverarbeitung

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Publikation

Kenton, P., Mur, L.A.J., Atzorn, R., Wasternack, C. & Draper, J. (—)-Jasmonic Acid Accumulation in Tobacco Hypersensitive Response Lesions Mol. Plant Microbiol. Interactions 12, 74-78, (1999) DOI: 10.1094/MPMI.1999.12.1.74

Tobacco infected with Pseudomonas syringae pv. phaseolicola undergoes a hypersensitive response (HR). Jasmonic acid (JA) accumulated within the developing lesion 3 to 9 h after infection and this accumulation preceded protein loss, cell death, and malondialdehyde accumulation. Accumulating JA consisted largely of the (—)-JA stereoisomer and was essentially restricted to the HR lesion

Publikation

Gago, S., Costa, N., Semorile, L. & Grau, O. Sequence variability in p27 gene of Citrus tristeza virus (CTV) revealed by SSCP analysis Electronic Journal of Biotechnology 2, 41-50, (1999)

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Publikation

Kramell, R., Miersch, O., Schneider, G. & Wasternack, C. Liquid chromatography of jasmonic acid amine conjugates Chromatographia 49, 42-46, (1999)

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Publikation

Herde, O., Peña-Cortés, H., Wasternack, C., Willmitzer, L. & Fisahn, J. Electric signaling and PIN2 gene expression on different abiotic stimuli depend on a distinct threshold level of endogenous ABA in several ABA-deficient tomato mutants Plant Physiol. 119, 213-218, (1999)

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Publikation

Miersch, O., Bohlmann, H. & Wasternack, C. Jasmonates and related compounds form Fusarium oxysporum Phytochemistry 50, 517-523, (1999)

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Publikation

Miersch, O., Kramell, R., Parthier, B. & Wasternack, C. Structure-activity relations of substituted, deleted or stereospecifically altered jasmonic acid in gene expression of barley leaves Phytochemistry 50, 353-361, (1999)

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Publikation

Morgan, K.E., Zarembinski, T.I., Theologis, A. & Abel, S. Biochemical characterization of recombinant polypeptides corresponding to the predicted ßαα-fold in Aux/IAA proteins FEBS Letters 454, 283-287, (1999)

The plant hormone indoleacetic acid (IAA or auxin) transcriptionally activates a select set of early genes. The Auxl IAA class of early auxin-responsive genes encodes a large family of short-lived, nuclear proteins. Aux/IAA polypeptides homo-and heterodimerize, and interact with auxin-response transcription factors (ARFs) via C-terminal regions conserved in both protein families. This shared region contains a predicted βαα motif similar to the prokaryotic β-Ribbon DNA binding domain, which mediates both protein dimerization and DNA recognition. Here, we show by circular dichroism spectroscopy and by chemical cross-linking experiments that recombinant peptides corresponding to the predicted βαα region of three Aux/IAA proteins from Arabidopsis thaliana contain substantial α-helical secondary structure and undergo homo- and heterotypic interactions in vitro. Our results indicate a similar biochemical function of the plant βαα domain and suggest that the βαα fold plays an important role in mediating combinatorial interactions of Aux/IAA and ARF proteins to specifically regulate secondary gene expression in response to auxin.

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