4ude

An oligomerization domain confers pioneer properties to the LEAFY master floral regulator

spinqualitylabelsall models 4ude, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ude is a 2 chain structure with sequence from Ginkgo biloba. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Ligands: GOL, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9LLY6_GINBI Publication Abstract from PubMed 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. A SAM oligomerization domain shapes the genomic binding landscape of the LEAFY transcription factor.,Sayou C, Nanao MH, Jamin M, Pose D, Thevenon E, Gregoire L, Tichtinsky G, Denay G, Ott F, Peirats Llobet M, Schmid M, Dumas R, Parcy F Nat Commun. 2016 Apr 21;7:11222. doi: 10.1038/ncomms11222. PMID:27097556 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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