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http://purl.uniprot.org/citations/23644595http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23644595http://www.w3.org/2000/01/rdf-schema#comment"IscR from Escherichia coli is an unusual metalloregulator in that both apo and iron sulfur (Fe-S)-IscR regulate transcription and exhibit different DNA binding specificities. Here, we report structural and biochemical studies of IscR suggesting that remodeling of the protein-DNA interface upon Fe-S ligation broadens the DNA binding specificity of IscR from binding the type 2 motif only to both type 1 and type 2 motifs. Analysis of an apo-IscR variant with relaxed target-site discrimination identified a key residue in wild-type apo-IscR that, we propose, makes unfavorable interactions with a type 1 motif. Upon Fe-S binding, these interactions are apparently removed, thereby allowing holo-IscR to bind both type 1 and type 2 motifs. These data suggest a unique mechanism of ligand-mediated DNA site recognition, whereby metallocluster ligation relocates a protein-specificity determinant to expand DNA target-site selection, allowing a broader transcriptomic response by holo-IscR."xsd:string
http://purl.uniprot.org/citations/23644595http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.2568"xsd:string
http://purl.uniprot.org/citations/23644595http://purl.uniprot.org/core/author"Zwart P.H."xsd:string
http://purl.uniprot.org/citations/23644595http://purl.uniprot.org/core/author"Brennan R.G."xsd:string
http://purl.uniprot.org/citations/23644595http://purl.uniprot.org/core/author"Rajagopalan S."xsd:string
http://purl.uniprot.org/citations/23644595http://purl.uniprot.org/core/author"Kiley P.J."xsd:string
http://purl.uniprot.org/citations/23644595http://purl.uniprot.org/core/author"Phillips K.J."xsd:string
http://purl.uniprot.org/citations/23644595http://purl.uniprot.org/core/author"Teter S.J."xsd:string
http://purl.uniprot.org/citations/23644595http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23644595http://purl.uniprot.org/core/name"Nat Struct Mol Biol"xsd:string
http://purl.uniprot.org/citations/23644595http://purl.uniprot.org/core/pages"740-747"xsd:string
http://purl.uniprot.org/citations/23644595http://purl.uniprot.org/core/title"Studies of IscR reveal a unique mechanism for metal-dependent regulation of DNA binding specificity."xsd:string
http://purl.uniprot.org/citations/23644595http://purl.uniprot.org/core/volume"20"xsd:string
http://purl.uniprot.org/citations/23644595http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23644595
http://purl.uniprot.org/citations/23644595http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23644595
http://purl.uniprot.org/uniprot/P0AGK8#attribution-B014725F9947A017AA4609516950A609http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/23644595
http://purl.uniprot.org/uniprot/#_P0AGK8-mappedCitation-23644595http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23644595
http://purl.uniprot.org/uniprot/P0AGK8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23644595