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http://purl.uniprot.org/citations/17032657http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17032657http://www.w3.org/2000/01/rdf-schema#comment"The Dna2 protein is a multifunctional enzyme with 5'-3' DNA helicase, DNA-dependent ATPase, 3' exo/endonuclease, and 5' exo/endonuclease. The enzyme is highly specific for structures containing single-stranded flaps adjacent to duplex regions. We report here two novel activities of both the yeast and human Dna2 helicase/nuclease protein: single strand annealing and ATP-independent strand exchange on short duplexes. These activities are independent of ATPase/helicase and nuclease activities in that mutations eliminating either nuclease or ATPase/helicase do not inhibit strand annealing or strand exchange. ATP inhibits strand exchange. A model rationalizing the multiple catalytic functions of Dna2 and leading to its coordination with other enzymes in processing single-stranded flaps during DNA replication and repair is presented."xsd:string
http://purl.uniprot.org/citations/17032657http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m604925200"xsd:string
http://purl.uniprot.org/citations/17032657http://purl.uniprot.org/core/author"Campbell J.L."xsd:string
http://purl.uniprot.org/citations/17032657http://purl.uniprot.org/core/author"Masuda-Sasa T."xsd:string
http://purl.uniprot.org/citations/17032657http://purl.uniprot.org/core/author"Polaczek P."xsd:string
http://purl.uniprot.org/citations/17032657http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17032657http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/17032657http://purl.uniprot.org/core/pages"38555-38564"xsd:string
http://purl.uniprot.org/citations/17032657http://purl.uniprot.org/core/title"Single strand annealing and ATP-independent strand exchange activities of yeast and human DNA2: possible role in Okazaki fragment maturation."xsd:string
http://purl.uniprot.org/citations/17032657http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/17032657http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17032657
http://purl.uniprot.org/citations/17032657http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17032657
http://purl.uniprot.org/uniprot/#_A0A8H4FBD9-mappedCitation-17032657http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17032657
http://purl.uniprot.org/uniprot/#_P38859-mappedCitation-17032657http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17032657
http://purl.uniprot.org/uniprot/#_P51530-mappedCitation-17032657http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17032657
http://purl.uniprot.org/uniprot/A0A8H4FBD9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17032657
http://purl.uniprot.org/uniprot/P38859http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17032657
http://purl.uniprot.org/uniprot/P51530http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17032657