4CHK

Crystal Structure of the ARF5 oligomerization domain

Summary for 4CHK

• Entry DOI: 10.2210/pdb4chk/pdb
• Descriptor: AUXIN RESPONSE FACTOR 5 (2 entities in total)
• Functional Keywords: pb1, transcription
• Biological source: ARABIDOPSIS THALIANA (THALE CRESS)
• Cellular location: Nucleus: P93024
• Total number of polymer chains: 8
• Total formula weight: 112687.98

Authors

Nanao, M.H.,Mazzoleni, M.,Thevenon, E.,Brunoud, G.,Vernoux, T.,Parcy, F.,Dumas, R. (deposition date: 2013-12-03, release date: 2014-04-16, Last modification date: 2024-05-08)

Primary citation

Nanao, M.H.,Vinos-Poyo, T.,Brunoud, G.,Thevenon, E.,Mazzoleni, M.,Mast, D.,Laine, S.,Wang, S.,Hagen, G.,Li, H.,Guilfoyle, T.J.,Parcy, F.,Vernoux, T.,Dumas, R.
Structural Basis for Oligomerisation of Auxin Transcriptional Regulators
Nat.Commun., 5:3617-, 2014

PubMed 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.

PubMed: 24710426
DOI: 10.1038/NCOMMS4617

Experimental method

X-RAY DIFFRACTION (2.85 Å)