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http://purl.uniprot.org/citations/21700224http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21700224http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21700224http://www.w3.org/2000/01/rdf-schema#comment"We present a molecular dissection of pause site-dependent transcriptional termination for mammalian RNA polymerase II (Pol II)-transcribed genes. We show that nascent transcripts form RNA/DNA hybrid structures (R-loops) behind elongating Pol II and are especially prevalent over G-rich pause sites positioned downstream of gene poly(A) signals. Senataxin, a helicase protein associated with AOA2/ALS4 neurodegenerative disorders, acts to resolve these R-loop structures and by so doing allows access of the 5'-3' exonuclease Xrn2 at 3' cleavage poly(A) sites. This affords 3' transcript degradation and consequent Pol II termination. In effect, R-loops formed over G-rich pause sites, followed by their resolution by senataxin, are key steps in the termination process."xsd:string
http://purl.uniprot.org/citations/21700224http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2011.04.026"xsd:string
http://purl.uniprot.org/citations/21700224http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2011.04.026"xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/author"Proudfoot N.J."xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/author"Proudfoot N.J."xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/author"Gromak N."xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/author"Gromak N."xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/author"Skourti-Stathaki K."xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/author"Skourti-Stathaki K."xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/pages"794-805"xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/pages"794-805"xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/title"Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination."xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/title"Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination."xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/volume"42"xsd:string
http://purl.uniprot.org/citations/21700224http://purl.uniprot.org/core/volume"42"xsd:string
http://purl.uniprot.org/citations/21700224http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21700224
http://purl.uniprot.org/citations/21700224http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21700224
http://purl.uniprot.org/citations/21700224http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21700224
http://purl.uniprot.org/citations/21700224http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21700224