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Wasternack, C. (8)Brandt, W. (5)Miersch, O. (5)Feussner, I. (4)Hause, B. (4)Strack, D. (4)Vogt, T. (4)Clemens, S. (3)Kramell, R. (3)Milkowski, C. (3)Feussner, K. (2)Lukačin, R. (2)Matern, U. (2)Scheel, D. (2)Specker, S. (2)Stehle, F. (2)Stenzel, I. (2)Abel, S. (1)Apel, K. (1)Arnold, U. (1)BERGER, S. (1)Baldwin, I. T. (1)Bauer, N. (1)Baumert, A. (1)Biastoff, S. (1)Bohlmann, H. (1)Boland, W. (1)Börner, T. (1)Böttcher, C. (1)Bücking, H. (1)Carbonell, A. (1)Cazalé, A.-C. (1)Churin, J. (1)De Luca, V. (1)De la Peña, M. (1)Delgado, S. (1)Dräger, B. (1)Dunaeva, M. (1)Ebel, J. (1)Flores, R. (1)Förster, H. (1)Gago, S. (1)Gas, M.-E. (1)Grzam, A. (1)Guranowski, A. (1)Göbel, C. (1)Görschen, E. (1)Hehmann, M. (1)Hell, R. (1)Herrmann, G. (1)Hertel, S. C. (1)Hilpert, B. (1)Hölscher, D. (1)Kaltenbach, M. (1)Kandzia, R. (1)Knöfel, H.-D. (1)Kutchan, T. M. (1)Kühn, H. (1)Lee, J. (1)Leopold, I. (1)Manke, K. (1)Maucher, H. (1)Maucher, H. P. (1)Meyer, A. J. (1)Mithöfer, A. (1)Molina, D. (1)Morgan, K. E. (1)Nennstiel, D. (1)Nürnberger, T. (1)Ortel, B. (1)Parthier, B. (1)Peumans, W. J. (1)Ranf, S. (1)Reeh, I. (1)Reinhardt, N. (1)Reva, V. (1)Rosahl, S. (1)Santos, J. G. (1)Schmidt, J. (1)Schneider, B. (1)Schröder, G. (1)Schröder, J. (1)Schüler, G. (1)Solé, M. (1)Staswick, P. E. (1)Stumpe, M. (1)Suza, W. (1)Tennstedt, P. (1)Theologis, A. (1)Trampczynska, A. (1)Trempel, F. (1)Unterbusch, E. (1)Vignutelli, A. (1)Westphal, L. (1)Wils, C. R. (1)
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Publikation
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.