Structural basis for oligomerization of auxin transcriptional regulators

Max H. Nanao, Thomas Vinos-Poyo, Géraldine Brunoud, Emmanuel Thévenon, Meryl Mazzoleni, David Mast, Stéphanie Lainé, Shucai Wang, Gretchen Hagen, Hanbing Li, Thomas J. Guilfoyle, François Parcy (), Teva Vernoux () and Renaud Dumas
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Max H. Nanao: European Molecular Biology Laboratory
Thomas Vinos-Poyo: CNRS, Laboratoire de Physiologie Cellulaire and Végétale, UMR 5168
Géraldine Brunoud: Laboratoire de Reproduction et Développement des Plantes, CNRS, INRA, ENS Lyon, UCBL, Université de Lyon
Emmanuel Thévenon: CNRS, Laboratoire de Physiologie Cellulaire and Végétale, UMR 5168
Meryl Mazzoleni: CNRS, Laboratoire de Physiologie Cellulaire and Végétale, UMR 5168
David Mast: Laboratoire de Reproduction et Développement des Plantes, CNRS, INRA, ENS Lyon, UCBL, Université de Lyon
Stéphanie Lainé: Laboratoire de Reproduction et Développement des Plantes, CNRS, INRA, ENS Lyon, UCBL, Université de Lyon
Shucai Wang: Key Laboratory of Molecular Epigenetics of MOE, Institute of Genetics and Cytology, Institute of Grassland Science, Northeast Normal University
Gretchen Hagen: University of Missouri
Hanbing Li: University of Missouri
Thomas J. Guilfoyle: University of Missouri
François Parcy: CNRS, Laboratoire de Physiologie Cellulaire and Végétale, UMR 5168
Teva Vernoux: Laboratoire de Reproduction et Développement des Plantes, CNRS, INRA, ENS Lyon, UCBL, Université de Lyon
Renaud Dumas: CNRS, Laboratoire de Physiologie Cellulaire and Végétale, UMR 5168

Nature Communications, 2014, vol. 5, issue 1, 1-8

Abstract: Abstract The plant hormone auxin is a key morphogenetic regulator acting from embryogenesis onwards. Transcriptional events in response to auxin are mediated by the auxin response factor (ARF) transcription factors and the Aux/IAA (IAA) transcriptional repressors. At low auxin concentrations, IAA repressors associate with ARF proteins and recruit corepressors that prevent auxin-induced gene expression. At higher auxin concentrations, IAAs are degraded and ARFs become free to regulate auxin-responsive genes. The interaction between ARFs and IAAs is thus central to auxin signalling and occurs through the highly conserved domain III/IV present in both types of proteins. Here, we report the crystal structure of ARF5 domain III/IV and reveal the molecular determinants of ARF–IAA interactions. We further provide evidence that ARFs have the potential to oligomerize, a property that could be important for gene regulation in response to auxin.

Date: 2014
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DOI: 10.1038/ncomms4617

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