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http://purl.uniprot.org/citations/18501926http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18501926http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18501926http://www.w3.org/2000/01/rdf-schema#comment"The Escherichia coli chromosomal relBE operon encodes a toxin-antitoxin system, which is autoregulated by its protein products, RelB and RelE. RelB acts as a transcriptional repressor and RelE functions as a cofactor to enhance the repressor activity of RelB. Here, we present the NMR-derived structure of a RelB dimer and show that a RelB dimer recognizes a hexad repeat in the palindromic operator region through a ribbon-helix-helix motif. Our biochemical data show that two weakly associated RelB dimers bind to the adjacent repeats in the 3'-site of the operator (O(R)) at a moderate affinity (K(d), approximately 10(-5) M). However, in the presence of RelE, a RelB tetramer binds two distinct binding sites within the operator region, each with an enhanced affinity (K(d), approximately 10(-6) M for the low-affinity site, O(L), and 10(-8) M for the high-affinity site, O(R)). We propose that the enhanced affinity for the operator element is mediated by a cooperative DNA binding by a pair of RelB dimers and that the interaction between RelB dimers is strongly augmented by the presence of the cognate toxin RelE."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2008.04.039"xsd:string
http://purl.uniprot.org/citations/18501926http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2008.04.039"xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/author"Inouye M."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/author"Inouye M."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/author"Li G.Y."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/author"Li G.Y."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/author"Ikura M."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/author"Ikura M."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/pages"107-119"xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/pages"107-119"xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/title"Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/title"Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module."xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/volume"380"xsd:string
http://purl.uniprot.org/citations/18501926http://purl.uniprot.org/core/volume"380"xsd:string
http://purl.uniprot.org/citations/18501926http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18501926
http://purl.uniprot.org/citations/18501926http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18501926