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Nat Commun. 2014 Apr 7;5:3617. doi: 10.1038/ncomms4617.

Structural basis for oligomerization of auxin transcriptional regulators.

Author information

1
1] European Molecular Biology Laboratory, 6 rue Jules Horowitz, BP 181, Grenoble 38042, France [2] Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 6 rue Jules Horowitz, Grenoble Cedex 9 38042, France.
2
1] CNRS, Laboratoire de Physiologie Cellulaire and Végétale, UMR 5168, Grenoble 38054, France [2] Univ. Grenoble Alpes, LPCV, Grenoble F-38054, France [3] CEA, DSV, iRTSV, LPCV, Grenoble F-38054, France [4] INRA, LPCV, Grenoble F-38054, France [5].
3
1] Laboratoire de Reproduction et Développement des Plantes, CNRS, INRA, ENS Lyon, UCBL, Université de Lyon, Lyon 69364, France [2].
4
1] CNRS, Laboratoire de Physiologie Cellulaire and Végétale, UMR 5168, Grenoble 38054, France [2] Univ. Grenoble Alpes, LPCV, Grenoble F-38054, France [3] CEA, DSV, iRTSV, LPCV, Grenoble F-38054, France [4] INRA, LPCV, Grenoble F-38054, France.
5
Laboratoire de Reproduction et Développement des Plantes, CNRS, INRA, ENS Lyon, UCBL, Université de Lyon, Lyon 69364, France.
6
Key Laboratory of Molecular Epigenetics of MOE, Institute of Genetics and Cytology, Institute of Grassland Science, Northeast Normal University, Changchun 130024, China.
7
Department of Biochemistry, University of Missouri, Columbia, Missouri 65211, USA.

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.

PMID:
24710426
DOI:
10.1038/ncomms4617
[Indexed for MEDLINE]

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