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http://purl.uniprot.org/citations/8262948http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8262948http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8262948http://www.w3.org/2000/01/rdf-schema#comment"DNA polymerase exonucleolytic proofreading is important in attaining high fidelity DNA replication. One of the most well characterized proofreading activities is the 3'-->5'-exonuclease activity of bacteriophage T4 DNA polymerase. We have used genetic analyses and protein sequence comparisons to Escherichia coli DNA polymerase I to identify amino acids in the N-terminal region of T4 DNA polymerase that are required for exonucleolytic proofreading. Mutant DNA polymerases with amino acid substitutions D112A/E114A, D219A, or D324A reduced 3'-->5'-exonuclease activity 10(2)-10(4)-fold in various in vitro assays and decreased DNA replication fidelity in vivo. DNA replication activity was also reduced for the exonuclease-deficient DNA polymerases in vitro and in vivo. Reduction in DNA replication appeared to be due primarily to the interdependence of T4 DNA polymerase replication and proofreading activities; T4 DNA polymerase requires 3'-->5'-exonuclease activity to repair primer termini that are not suitable substrates for extension. Observations reported here provide further evidence in support of the proposal that DNA polymerases have distinct 3'-->5'-exonuclease and polymerase active sites."xsd:string
http://purl.uniprot.org/citations/8262948http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)74223-9"xsd:string
http://purl.uniprot.org/citations/8262948http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)74223-9"xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/author"Nonay R.L."xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/author"Nonay R.L."xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/author"Reha-Krantz L.J."xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/author"Reha-Krantz L.J."xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/pages"27100-27108"xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/pages"27100-27108"xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/title"Genetic and biochemical studies of bacteriophage T4 DNA polymerase 3'-->5'-exonuclease activity."xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/title"Genetic and biochemical studies of bacteriophage T4 DNA polymerase 3'-->5'-exonuclease activity."xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/volume"268"xsd:string
http://purl.uniprot.org/citations/8262948http://purl.uniprot.org/core/volume"268"xsd:string
http://purl.uniprot.org/citations/8262948http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8262948
http://purl.uniprot.org/citations/8262948http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8262948
http://purl.uniprot.org/citations/8262948http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8262948
http://purl.uniprot.org/citations/8262948http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8262948
http://purl.uniprot.org/uniprot/P04415http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8262948
http://purl.uniprot.org/uniprot/P04415#attribution-164F157DE1F3522A4BFC4A31947EAAC0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/8262948