http://purl.uniprot.org/citations/19033358 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19033358 | http://www.w3.org/2000/01/rdf-schema#comment | "Previous studies showed that the K342E substitution in the Saccharomyces cerevisiae Rad51 protein increases the interaction with Rad54 protein in the two-hybrid system, leads to increased sensitivity to the alkylating agent MMS and hyper-recombination in an oligonucleotide-mediated gene targeting assay. K342 localizes in loop 2, a region of Rad51 whose function is not well understood. Here, we show that Rad51-K342E displays DNA-independent and DNA-dependent ATPase activities, owing to its ability to form filaments in the absence of a DNA lattice. These filaments exhibit a compressed pitch of 81 A, whereas filaments of wild-type Rad51 and Rad51-K342E on DNA form extended filaments with a 97 A pitch. Rad51-K342E shows near normal binding to ssDNA, but displays a defect in dsDNA binding, resulting in less stable protein-dsDNA complexes. The mutant protein is capable of catalyzing the DNA strand exchange reaction and is insensitive to inhibition by the early addition of dsDNA. Wild-type Rad51 protein is inhibited under such conditions, because of its ability to bind dsDNA. No significant changes in the interaction between Rad51-K342E and Rad54 could be identified. These findings suggest that loop 2 contributes to the primary DNA-binding site in Rad51, controlling filament formation and ATPase activity."xsd:string |
http://purl.uniprot.org/citations/19033358 | http://purl.org/dc/terms/identifier | "doi:10.1093/nar/gkn914"xsd:string |
http://purl.uniprot.org/citations/19033358 | http://purl.uniprot.org/core/author | "Egelman E.H."xsd:string |
http://purl.uniprot.org/citations/19033358 | http://purl.uniprot.org/core/author | "Yu X."xsd:string |
http://purl.uniprot.org/citations/19033358 | http://purl.uniprot.org/core/author | "Zhang X.P."xsd:string |
http://purl.uniprot.org/citations/19033358 | http://purl.uniprot.org/core/author | "Heyer W.D."xsd:string |
http://purl.uniprot.org/citations/19033358 | http://purl.uniprot.org/core/author | "Galkin V.E."xsd:string |
http://purl.uniprot.org/citations/19033358 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19033358 | http://purl.uniprot.org/core/name | "Nucleic Acids Res"xsd:string |
http://purl.uniprot.org/citations/19033358 | http://purl.uniprot.org/core/pages | "158-171"xsd:string |
http://purl.uniprot.org/citations/19033358 | http://purl.uniprot.org/core/title | "Loop 2 in Saccharomyces cerevisiae Rad51 protein regulates filament formation and ATPase activity."xsd:string |
http://purl.uniprot.org/citations/19033358 | http://purl.uniprot.org/core/volume | "37"xsd:string |
http://purl.uniprot.org/citations/19033358 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19033358 |
http://purl.uniprot.org/citations/19033358 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19033358 |
http://purl.uniprot.org/uniprot/#_A0A8H8ULW3-mappedCitation-19033358 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19033358 |
http://purl.uniprot.org/uniprot/#_P25454-mappedCitation-19033358 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19033358 |
http://purl.uniprot.org/uniprot/A0A8H8ULW3 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19033358 |
http://purl.uniprot.org/uniprot/P25454 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19033358 |