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http://purl.uniprot.org/citations/20383123http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20383123http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20383123http://www.w3.org/2000/01/rdf-schema#comment"Mammalian cells require non-homologous end joining (NHEJ) for the efficient repair of chromosomal DNA double-strand breaks. A key feature of biological sources of strand breaks is associated nucleotide damage, including base loss (abasic or apurinic/apyrimidinic (AP) sites). At single-strand breaks, 5'-terminal abasic sites are excised by the 5'-deoxyribose-5-phosphate (5'-dRP) lyase activity of DNA polymerase beta (pol beta): here we show, in vitro and in cells, that accurate and efficient repair by NHEJ of double-strand breaks with such damage similarly requires 5'-dRP/AP lyase activity. Classically defined NHEJ is moreover uniquely effective at coupling this end-cleaning step to joining in cells, helping to distinguish this pathway from otherwise robust alternative NHEJ pathways. The NHEJ factor Ku can be identified as an effective 5'-dRP/AP lyase. In a similar manner to other lyases, Ku nicks DNA 3' of an abasic site by a mechanism involving a Schiff-base covalent intermediate with the abasic site. We show by using cell extracts that Ku is essential for the efficient removal of AP sites near double-strand breaks and, consistent with this result, that joining of such breaks is specifically decreased in cells complemented with a lyase-attenuated Ku mutant. Ku had previously been presumed only to recognize ends and recruit other factors that process ends; our data support an unexpected direct role for Ku in end-processing steps as well."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.org/dc/terms/identifier"doi:10.1038/nature08926"xsd:string
http://purl.uniprot.org/citations/20383123http://purl.org/dc/terms/identifier"doi:10.1038/nature08926"xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Roberts S.A."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Roberts S.A."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Ramsden D.A."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Ramsden D.A."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Burkhalter M.D."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Burkhalter M.D."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Havener J.M."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Havener J.M."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Hasty P."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Hasty P."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Strande N."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Strande N."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Strom C."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/author"Strom C."xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/pages"1214-1217"xsd:string
http://purl.uniprot.org/citations/20383123http://purl.uniprot.org/core/pages"1214-1217"xsd:string