5nqs | pdb_00005nqs

Structure of the Arabidopsis Thaliana TOPLESS N-terminal domain

spinqualitylabelsall models 5nqs, resolution 2.61Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nqs is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.61Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TPL_ARATH Transcriptional corepressor. May repress the expression of root-promoting genes in the top half of the embryo to allow proper differentiation of the shoot pole during the transition stage of embryogenesis. Regulates the expression of PLT1 and PLT2. Negative regulator of jasmonate responses. Negative regulator of auxin responses. Negative regulator of multiple floral organ identity genes (PubMed:23034631). Required for ovule development (PubMed:25378179). Publication Abstract from PubMed Transcriptional repression involves a class of proteins called corepressors that link transcription factors to chromatin remodeling complexes. In plants such as Arabidopsis thaliana, the most prominent corepressor is TOPLESS (TPL), which plays a key role in hormone signaling and development. Here we present the crystallographic structure of the Arabidopsis TPL N-terminal region comprising the LisH and CTLH (C-terminal to LisH) domains and a newly identified third region, which corresponds to a CRA domain. Comparing the structure of TPL with the mammalian TBL1, which shares a similar domain structure and performs a parallel corepressor function, revealed that the plant TPLs have evolved a new tetramerization interface and unique and highly conserved surface for interaction with repressors. Using site-directed mutagenesis, we validated those surfaces in vitro and in vivo and showed that TPL tetramerization and repressor binding are interdependent. Our results illustrate how evolution used a common set of protein domains to create a diversity of corepressors, achieving similar properties with different molecular solutions. Structure of the Arabidopsis TOPLESS corepressor provides insight into the evolution of transcriptional repression.,Martin-Arevalillo R, Nanao MH, Larrieu A, Vinos-Poyo T, Mast D, Galvan-Ampudia C, Brunoud G, Vernoux T, Dumas R, Parcy F Proc Natl Acad Sci U S A. 2017 Jul 25;114(30):8107-8112. doi:, 10.1073/pnas.1703054114. Epub 2017 Jul 11. PMID:28698367 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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