RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/17435766http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17435766http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17435766http://www.w3.org/2000/01/rdf-schema#comment"H-NS is a protein of the bacterial nucleoid involved in DNA compaction and transcription regulation. In vivo, H-NS selectively silences specific genes of the bacterial chromosome. However, many studies have concluded that H-NS binds sequence-independently to DNA, leaving the molecular basis for its selectivity unexplained. We show that the negative regulatory element (NRE) of the supercoiling-sensitive Escherichia coliproU gene contains two identical high-affinity binding sites for H-NS. Cooperative binding of H-NS is abrogated by changes in DNA superhelical density and temperature. We further demonstrate that the high-affinity sites nucleate cooperative binding and establish a nucleoprotein structure required for silencing. Mutations in these sites result in loss of repression by H-NS. In this model, silencing at proU, and by inference at other genes directly regulated by H-NS, is tightly controlled by the cooperativity between bound H-NS molecules."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.org/dc/terms/identifier"doi:10.1038/nsmb1233"xsd:string
http://purl.uniprot.org/citations/17435766http://purl.org/dc/terms/identifier"doi:10.1038/nsmb1233"xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/author"Travers A."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/author"Travers A."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/author"Badaut C."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/author"Badaut C."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/author"Rimsky S."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/author"Rimsky S."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/author"Bouffartigues E."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/author"Bouffartigues E."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/author"Buckle M."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/author"Buckle M."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/pages"441-448"xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/pages"441-448"xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/title"H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/title"H-NS cooperative binding to high-affinity sites in a regulatory element results in transcriptional silencing."xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/17435766http://purl.uniprot.org/core/volume"14"xsd:string