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http://purl.uniprot.org/citations/11863428http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11863428http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11863428http://www.w3.org/2000/01/rdf-schema#comment"Werner syndrome is a rare autosomal recessive disease characterized by a premature aging phenotype, genomic instability, and a dramatically increased incidence of cancer and heart disease. Mutations in a single gene encoding a 1432-amino acid helicase/exonuclease (hWRN) have been shown to be responsible for the development of this disease. We have cloned, overexpressed, and purified a minimal, 171-amino acid fragment of hWRN that functions as an exonuclease. This fragment, encompassing residues 70-240 of hWRN (hWRN-N(70-240)), exhibits the same level of 3'-5' exonuclease activity as the previously described exonuclease fragment encompassing residues 1-333 of the full-length protein. The fragment also contains a 5'-protruding DNA strand endonuclease activity at a single-strand-double-strand DNA junction and within single-stranded DNA, as well as a 3'-5' exonuclease activity on single-stranded DNA. We find hWRN-N(70-240) is in a trimer-hexamer equilibrium in the absence of DNA when examined by gel filtration chromatography and atomic force microscopy. Upon addition of DNA substrate, hWRN-N(70-240) forms a hexamer and interacts with the recessed 3'-end of the DNA. Moreover, we find that the interaction of hWRN-N(70-240) with the replication protein PCNA also causes this minimal, 171-amino acid exonuclease region to form a hexamer. Thus, the active form of this minimal exonuclease fragment of human WRN appears to be a hexamer. The implications these results have on our understanding of hWRN's roles in DNA replication and repair are discussed."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.org/dc/terms/identifier"doi:10.1021/bi0157161"xsd:string
http://purl.uniprot.org/citations/11863428http://purl.org/dc/terms/identifier"doi:10.1021/bi0157161"xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Xue Y."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Xue Y."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Wang H."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Wang H."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Redinbo M.R."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Redinbo M.R."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Gray M.D."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Gray M.D."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Erie D.A."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Erie D.A."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Davis-Searles P.R."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Davis-Searles P.R."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Ratcliff G.C."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/author"Ratcliff G.C."xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/pages"2901-2912"xsd:string
http://purl.uniprot.org/citations/11863428http://purl.uniprot.org/core/pages"2901-2912"xsd:string