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http://purl.uniprot.org/citations/25171413http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25171413http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25171413http://www.w3.org/2000/01/rdf-schema#comment"The cyclic dinucleotide c-di-GMP is a signaling molecule with diverse functions in cellular physiology. Here, we report that c-di-GMP can assemble into a tetramer that mediates the effective dimerization of a transcription factor, BldD, which controls the progression of multicellular differentiation in sporulating actinomycete bacteria. BldD represses expression of sporulation genes during vegetative growth in a manner that depends on c-di-GMP-mediated dimerization. Structural and biochemical analyses show that tetrameric c-di-GMP links two subunits of BldD through their C-terminal domains, which are otherwise separated by ~10 Å and thus cannot effect dimerization directly. Binding of the c-di-GMP tetramer by BldD is selective and requires a bipartite RXD-X8-RXXD signature. The findings indicate a unique mechanism of protein dimerization and the ability of nucleotide signaling molecules to assume alternative oligomeric states to effect different functions."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2014.07.022"xsd:string
http://purl.uniprot.org/citations/25171413http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2014.07.022"xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Buttner M.J."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Buttner M.J."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Brennan R.G."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Brennan R.G."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Schumacher M.A."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Schumacher M.A."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Tschowri N."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Tschowri N."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Schlimpert S."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Schlimpert S."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Findlay K.C."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Findlay K.C."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Chinnam N.B."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/author"Chinnam N.B."xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/pages"1136-1147"xsd:string
http://purl.uniprot.org/citations/25171413http://purl.uniprot.org/core/pages"1136-1147"xsd:string