| http://purl.uniprot.org/citations/16737853 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16737853 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16737853 | http://www.w3.org/2000/01/rdf-schema#comment | "Previous studies have shown that human ribosomal protein S3 (hS3) has a high apparent binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG) residues in DNA and interacts with the human base excision repair (BER) proteins OGG1 and APE/Ref-1. We used a combination of computational and experimental approaches to understand the role of hS3 in BER and its potential to hinder repair of 8-oxoG lesions by OGG1 and APE/Ref-1. Sequence analysis was employed to identify hS3 residues likely to be involved in binding to 8-oxoG. One putative site, lysine 132 (K132), located in a helix-hairpin-helix DNA binding motif, was mutated to alanine (K132A). The hS3-K132A mutant retained the ability to cleave abasic DNA, but its capacity to bind 8-oxoG was abrogated completely. The ability of OGG1 to cleave an 8-oxoG-oligonucleotide substrate pre-incubated with hS3 or hS3-K132A was also tested. Pre-incubations with wild-type hS3 and 8-oxoG-containing oligonucleotides completely prevented the subsequent removal of 8-oxoG by OGG1. On the other hand, OGG1 incubations combined with hS3-K132A stimulated cleavage of 8-oxoG in excess of two-fold, confirming previous observations that hS3 positively interacts with OGG1, but only under conditions in which the binding of hS3 to 8-oxoG is limited. Overall, the ability of OGG1 to repair 8-oxoG is compromised when hS3 is bound to 8-oxoG sites. Conversely, in the absence of DNA binding, hS3 interacts positively with OGG1 to produce a more robust removal of 8-oxoG residues in DNA."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.dnarep.2006.04.001"xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.dnarep.2006.04.001"xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/author | "Wang M."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/author | "Wang M."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/author | "Deutsch W.A."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/author | "Deutsch W.A."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/author | "Hegde V."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/author | "Hegde V."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/author | "Mian I.S."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/author | "Mian I.S."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/author | "Spyres L."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/author | "Spyres L."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/date | "2006"xsd:gYear |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/name | "DNA Repair"xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/name | "DNA Repair"xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/pages | "810-815"xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/pages | "810-815"xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/title | "The high binding affinity of human ribosomal protein S3 to 7,8-dihydro-8-oxoguanine is abrogated by a single amino acid change."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/title | "The high binding affinity of human ribosomal protein S3 to 7,8-dihydro-8-oxoguanine is abrogated by a single amino acid change."xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/volume | "5"xsd:string |
| http://purl.uniprot.org/citations/16737853 | http://purl.uniprot.org/core/volume | "5"xsd:string |