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http://purl.uniprot.org/citations/15546877http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15546877http://www.w3.org/2000/01/rdf-schema#comment"The Saccharomyces cerevisiae Rad50-Mre11-Xrs2 complex plays a central role in the cellular response to DNA double strand breaks. Rad50 has a globular ATPase head domain with a long coiled-coil tail. DNA binding by Rad50 is ATP-dependent and the Rad50-Mre11-Xrs2 complex possesses DNA unwinding and endonuclease activities that are regulated by ATP. Here we have examined the role of the Rad50 Walker type A ATP binding motif in DNA double strand break repair by a combination of genetic and biochemical approaches. Replacement of the conserved lysine residue within the Walker A motif with alanine, glutamate, or arginine results in the same DNA damage sensitivity and homologous recombination defect as the rad50 deletion mutation. The Walker A mutations also cause a deficiency in non-homologous end-joining. As expected, complexes containing the rad50 Walker A mutant proteins are defective in ATPase, ATP-dependent DNA unwinding, and ATP-stimulated endonuclease activities. Although the DNA end-bridging activity of the Rad50-Mre11-Xrs2 complex is ATP-independent, the end-bridging activity of complexes containing the rad50 Walker A mutant proteins is salt-sensitive. These results provide a molecular explanation for the observed in vivo defects of the rad50 Walker mutant strains and reveal a novel ATP-independent function for Rad50 in DNA end-bridging."xsd:string
http://purl.uniprot.org/citations/15546877http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m410192200"xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/author"Chen L."xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/author"Tomkinson A.E."xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/author"Sung P."xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/author"Lewis L.K."xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/author"Resnick M.A."xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/author"Krejci L."xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/author"Van Komen S."xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/author"Trujillo K.M."xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/author"Roh D.H."xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/pages"2620-2627"xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/title"Effect of amino acid substitutions in the rad50 ATP binding domain on DNA double strand break repair in yeast."xsd:string
http://purl.uniprot.org/citations/15546877http://purl.uniprot.org/core/volume"280"xsd:string
http://purl.uniprot.org/citations/15546877http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15546877
http://purl.uniprot.org/citations/15546877http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15546877
http://purl.uniprot.org/uniprot/P12753#attribution-C8D3BA82189D2A5BE36D874F18910883http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15546877
http://purl.uniprot.org/uniprot/#_A0A8H4FAN2-mappedCitation-15546877http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15546877
http://purl.uniprot.org/uniprot/#_P12753-mappedCitation-15546877http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15546877
http://purl.uniprot.org/uniprot/A0A8H4FAN2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15546877
http://purl.uniprot.org/uniprot/P12753http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15546877