Structural basis for oligomerization of auxin transcriptional regulators.

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Nanao, Max H | Vinos-Poyo, Thomas | Brunoud, Géraldine | Thévenon, Emmanuel | Mazzoleni, Meryl | Mast, David | Lainé, Stéphanie | Wang, Shucai | Hagen, Gretchen | Li, Hanbing | Guilfoyle, Thomas J | Parcy, François | Vernoux, Teva | Dumas, Renaud

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Supplementary Information Supplementary Figures 1-3 and Supplementary Tables 1-2. International audience. 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.

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