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http://purl.uniprot.org/citations/10899134http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10899134http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10899134http://www.w3.org/2000/01/rdf-schema#comment"The FEN1 nuclease functions during Okazaki fragment maturation in the eukaryotic cell. Like many other proliferating cell nuclear antigen (PCNA)-binding proteins, FEN1 interacts with the interdomain connector loop (IDCL) of PCNA, and PCNA greatly stimulates FEN1 activity. A yeast IDCL mutant pcna-79 (IL126,128AA) failed to interact with FEN-1, but, surprisingly, pcna-79 was still very active in stimulating FEN1 activity. In contrast, a C-terminal mutant pcna-90 (PK252,253AA) showed wild-type binding to FEN1 in solution, but poorly stimulated FEN1 activity. When PCNA was loaded onto a DNA substrate coupled to magnetic beads, it stabilized retention of FEN1 on the DNA. In this DNA-dependent binding assay, pcna-79 also stabilized retention of FEN1, but pcna-90 was inactive. Therefore, in the absence of DNA, FEN1 interacts with PCNA mainly through the IDCL. However, when PCNA encircles the DNA, the C-terminal domain of PCNA rather than its IDCL is important for binding FEN1. An FF-->GA mutation in the PCNA-interaction domain of FEN1 severely decreased both modes of interaction with PCNA and resulted in replication and repair defects in vivo."xsd:string
http://purl.uniprot.org/citations/10899134http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.14.3811"xsd:string
http://purl.uniprot.org/citations/10899134http://purl.org/dc/terms/identifier"doi:10.1093/emboj/19.14.3811"xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/author"Burgers P.M."xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/author"Burgers P.M."xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/author"Gomes X.V."xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/author"Gomes X.V."xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/pages"3811-3821"xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/pages"3811-3821"xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/title"Two modes of FEN1 binding to PCNA regulated by DNA."xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/title"Two modes of FEN1 binding to PCNA regulated by DNA."xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/10899134http://purl.uniprot.org/core/volume"19"xsd:string
http://purl.uniprot.org/citations/10899134http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10899134
http://purl.uniprot.org/citations/10899134http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10899134
http://purl.uniprot.org/citations/10899134http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10899134
http://purl.uniprot.org/citations/10899134http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10899134
http://purl.uniprot.org/uniprot/P26793http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10899134
http://purl.uniprot.org/uniprot/P26793#attribution-E53F0F25B373C5E833BC8A0626B8D592http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/10899134