| http://purl.uniprot.org/citations/17208257 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17208257 | http://www.w3.org/2000/01/rdf-schema#comment | "The Saccharomyces cerevisiae Rad52 protein has a crucial role in the repair of DNA double-strand breaks by homologous recombination. In vitro, Rad52 displays DNA binding and strand annealing activities and promotes Rad51-mediated strand exchange. Schizosaccharomyces pombe has two Rad52 homologues, Rad22A and Rad22B. Whereas rad22A deficient strains exhibit severe defects in repair and recombination, rad22B mutants have a much less severe phenotype. To better understand the role of Rad22A and Rad22B in double-strand break repair, both proteins were purified to near homogeneity. Using gel retardation and filter binding assays, binding of Rad22A and Rad22B to short single-stranded DNAs was demonstrated. Binding of Rad22A to double-stranded oligonucleotides or linearized plasmid molecules containing blunt ends or short single-stranded overhangs could not be detected. Rad22B also does not bind efficiently to short duplex oligonucleotides but binds readily to DNA fragments containing 3'-overhangs. Rad22A as well as Rad22B efficiently promote annealing of complementary single-stranded DNAs. In the presence of Rad22A annealing of complementary DNAs is almost 90%. Whereas in reactions containing Rad22B the maximum level of annealing is 60%, most likely due to inhibition of the reaction by duplex DNA. Gel-filtration experiments and electron microscopic analyses indicate self-association of Rad22A and Rad22B and the formation of multimeric structures as has been observed for Rad52 in yeast and man."xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.mrfmmm.2006.11.032"xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://purl.uniprot.org/core/author | "Koning R.I."xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://purl.uniprot.org/core/author | "Pastink A."xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://purl.uniprot.org/core/author | "van Zeeland A.A."xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://purl.uniprot.org/core/author | "Zonneveld J.B."xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://purl.uniprot.org/core/author | "de Groot A.J."xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://purl.uniprot.org/core/author | "de Vries F.A."xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17208257 | http://purl.uniprot.org/core/name | "Mutat Res"xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://purl.uniprot.org/core/pages | "143-152"xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://purl.uniprot.org/core/title | "Schizosaccharomyces pombe Rad22A and Rad22B have similar biochemical properties and form multimeric structures."xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://purl.uniprot.org/core/volume | "615"xsd:string |
| http://purl.uniprot.org/citations/17208257 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17208257 |
| http://purl.uniprot.org/citations/17208257 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17208257 |
| http://purl.uniprot.org/uniprot/O42905#attribution-903163E451676556EAA96588A01A193A | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17208257 |
| http://purl.uniprot.org/uniprot/P36592#attribution-903163E451676556EAA96588A01A193A | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/17208257 |