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http://purl.uniprot.org/citations/19033358http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19033358http://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/19033358http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkn914"xsd:string
http://purl.uniprot.org/citations/19033358http://purl.uniprot.org/core/author"Egelman E.H."xsd:string
http://purl.uniprot.org/citations/19033358http://purl.uniprot.org/core/author"Yu X."xsd:string
http://purl.uniprot.org/citations/19033358http://purl.uniprot.org/core/author"Zhang X.P."xsd:string
http://purl.uniprot.org/citations/19033358http://purl.uniprot.org/core/author"Heyer W.D."xsd:string
http://purl.uniprot.org/citations/19033358http://purl.uniprot.org/core/author"Galkin V.E."xsd:string
http://purl.uniprot.org/citations/19033358http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19033358http://purl.uniprot.org/core/name"Nucleic Acids Res"xsd:string
http://purl.uniprot.org/citations/19033358http://purl.uniprot.org/core/pages"158-171"xsd:string
http://purl.uniprot.org/citations/19033358http://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/19033358http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/19033358http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19033358
http://purl.uniprot.org/citations/19033358http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19033358
http://purl.uniprot.org/uniprot/#_A0A8H8ULW3-mappedCitation-19033358http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19033358
http://purl.uniprot.org/uniprot/#_P25454-mappedCitation-19033358http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19033358
http://purl.uniprot.org/uniprot/A0A8H8ULW3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19033358
http://purl.uniprot.org/uniprot/P25454http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19033358