Structural basis for oligomerization of auxin transcriptional regulators.
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.
Mesh Terms:
Arabidopsis, Arabidopsis Proteins, Crystallography, X-Ray, DNA-Binding Proteins, Gene Expression Regulation, Plant, Indoleacetic Acids, Morphogenesis, Plant Growth Regulators, Protein Interaction Domains and Motifs, Protein Structure, Tertiary, Signal Transduction, Transcription Factors
Arabidopsis, Arabidopsis Proteins, Crystallography, X-Ray, DNA-Binding Proteins, Gene Expression Regulation, Plant, Indoleacetic Acids, Morphogenesis, Plant Growth Regulators, Protein Interaction Domains and Motifs, Protein Structure, Tertiary, Signal Transduction, Transcription Factors
Nat Commun
Date: Apr. 07, 2014
PubMed ID: 24710426
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