4UDE
An oligomerization domain confers pioneer properties to the LEAFY master floral regulator
Summary for 4UDE
| Entry DOI | 10.2210/pdb4ude/pdb |
| Descriptor | GINLFY PROTEIN, TETRAETHYLENE GLYCOL, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | sam, transcription, oligomerisation |
| Biological source | GINKGO BILOBA (MAIDENHAIR TREE) |
| Total number of polymer chains | 2 |
| Total formula weight | 25903.82 |
| Authors | Nanao, M.H.,Sayou, C.,Dumas, R.,Parcy, F. (deposition date: 2014-12-10, release date: 2016-03-02, Last modification date: 2024-05-08) |
| Primary citation | Sayou, C.,Nanao, M.H.,Jamin, M.,Pose, D.,Thevenon, E.,Gregoire, L.,Tichtinsky, G.,Denay, G.,Ott, F.,Peirats Llobet, M.,Schmid, M.,Dumas, R.,Parcy, F. A Sam Oligomerization Domain Shapes the Genomic Binding Landscape of the Leafy Transcription Factor Nat.Commun., 7:11222-, 2016 Cited by PubMed Abstract: Deciphering the mechanisms directing transcription factors (TFs) to specific genome regions is essential to understand and predict transcriptional regulation. TFs recognize short DNA motifs primarily through their DNA-binding domain. Some TFs also possess an oligomerization domain suspected to potentiate DNA binding but for which the genome-wide influence remains poorly understood. Here we focus on the LEAFY transcription factor, a master regulator of flower development in angiosperms. We have determined the crystal structure of its conserved amino-terminal domain, revealing an unanticipated Sterile Alpha Motif oligomerization domain. We show that this domain is essential to LEAFY floral function. Moreover, combined biochemical and genome-wide assays suggest that oligomerization is required for LEAFY to access regions with low-affinity binding sites or closed chromatin. This finding shows that domains that do not directly contact DNA can nevertheless have a profound impact on the DNA binding landscape of a TF. PubMed: 27097556DOI: 10.1038/NCOMMS11222 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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