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http://purl.uniprot.org/citations/28698367http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28698367http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28698367http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1703054114"xsd:string
http://purl.uniprot.org/citations/28698367http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1703054114"xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Dumas R."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Dumas R."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Parcy F."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Parcy F."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Brunoud G."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Brunoud G."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Larrieu A."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Larrieu A."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Nanao M.H."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Nanao M.H."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Vernoux T."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Vernoux T."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Galvan-Ampudia C."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Galvan-Ampudia C."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Martin-Arevalillo R."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Martin-Arevalillo R."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Mast D."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Mast D."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Vinos-Poyo T."xsd:string
http://purl.uniprot.org/citations/28698367http://purl.uniprot.org/core/author"Vinos-Poyo T."xsd:string