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http://purl.uniprot.org/citations/21386817http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21386817http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21386817http://www.w3.org/2000/01/rdf-schema#comment"Related RNA polymerases (RNAPs) carry out cellular gene transcription in all three kingdoms of life. The universal conservation of the transcription machinery extends to a single RNAP-associated factor, Spt5 (or NusG in bacteria), which renders RNAP processive and may have arisen early to permit evolution of long genes. Spt5 associates with Spt4 to form the Spt4/5 heterodimer. Here, we present the crystal structure of archaeal Spt4/5 bound to the RNAP clamp domain, which forms one side of the RNAP active centre cleft. The structure revealed a conserved Spt5-RNAP interface and enabled modelling of complexes of Spt4/5 counterparts with RNAPs from all kingdoms of life, and of the complete yeast RNAP II elongation complex with bound Spt4/5. The N-terminal NGN domain of Spt5/NusG closes the RNAP active centre cleft to lock nucleic acids and render the elongation complex stable and processive. The C-terminal KOW1 domain is mobile, but its location is restricted to a region between the RNAP clamp and wall above the RNA exit tunnel, where it may interact with RNA and/or other factors."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.org/dc/terms/identifier"doi:10.1038/emboj.2011.64"xsd:string
http://purl.uniprot.org/citations/21386817http://purl.org/dc/terms/identifier"doi:10.1038/emboj.2011.64"xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/author"Cramer P."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/author"Cramer P."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/author"Sainsbury S."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/author"Sainsbury S."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/author"Cheung A.C."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/author"Cheung A.C."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/author"Martinez-Rucobo F.W."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/author"Martinez-Rucobo F.W."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/pages"1302-1310"xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/pages"1302-1310"xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/title"Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/title"Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity."xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/volume"30"xsd:string
http://purl.uniprot.org/citations/21386817http://purl.uniprot.org/core/volume"30"xsd:string
http://purl.uniprot.org/citations/21386817http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21386817
http://purl.uniprot.org/citations/21386817http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21386817