2007
Conformational Changes during Normal and Error-Prone Incorporation of Nucleotides by a Y-Family DNA Polymerase Detected by 2-Aminopurine Fluorescence †
DeLucia A, Grindley N, Joyce C. Conformational Changes during Normal and Error-Prone Incorporation of Nucleotides by a Y-Family DNA Polymerase Detected by 2-Aminopurine Fluorescence †. Biochemistry 2007, 46: 10790-10803. PMID: 17725324, DOI: 10.1021/bi7006756.Peer-Reviewed Original Research2-AminopurineArchaeal ProteinsBase Pair MismatchBase SequenceDeoxyribonucleotidesDNA Polymerase betaDNA Polymerase IDNA RepairDNA ReplicationDNA-Directed DNA PolymeraseFluorescent DyesFrameshift MutationModels, MolecularMolecular Sequence DataMutagenesis, InsertionalNucleic Acid ConformationSpectrometry, FluorescenceSubstrate SpecificitySulfolobusTemplates, Genetic
2006
The Properties of Steric Gate Mutants Reveal Different Constraints within the Active Sites of Y-family and A-family DNA Polymerases*
DeLucia A, Chaudhuri S, Potapova O, Grindley N, Joyce C. The Properties of Steric Gate Mutants Reveal Different Constraints within the Active Sites of Y-family and A-family DNA Polymerases*. Journal Of Biological Chemistry 2006, 281: 27286-27291. PMID: 16831866, DOI: 10.1074/jbc.m604393200.Peer-Reviewed Original Research
2003
An error‐prone family Y DNA polymerase (DinB homolog from Sulfolobus solfataricus) uses a ‘steric gate’ residue for discrimination against ribonucleotides
DeLucia A, Grindley N, Joyce C. An error‐prone family Y DNA polymerase (DinB homolog from Sulfolobus solfataricus) uses a ‘steric gate’ residue for discrimination against ribonucleotides. Nucleic Acids Research 2003, 31: 4129-4137. PMID: 12853630, PMCID: PMC165950, DOI: 10.1093/nar/gkg417.Peer-Reviewed Original Research
2002
The Mutational Specificity of the Dbh Lesion Bypass Polymerase and Its Implications*
Potapova O, Grindley N, Joyce C. The Mutational Specificity of the Dbh Lesion Bypass Polymerase and Its Implications*. Journal Of Biological Chemistry 2002, 277: 28157-28166. PMID: 12023283, DOI: 10.1074/jbc.m202607200.Peer-Reviewed Original Research
1983
Construction of a plasmid that overproduces the large proteolytic fragment (Klenow fragment) of DNA polymerase I of Escherichia coli.
Joyce C, Grindley N. Construction of a plasmid that overproduces the large proteolytic fragment (Klenow fragment) of DNA polymerase I of Escherichia coli. Proceedings Of The National Academy Of Sciences Of The United States Of America 1983, 80: 1830-1834. PMID: 6340110, PMCID: PMC393703, DOI: 10.1073/pnas.80.7.1830.Peer-Reviewed Original ResearchMeSH KeywordsCloning, MolecularDNA Polymerase IDNA-Directed DNA PolymeraseEscherichia coliGene Expression RegulationLac OperonOperonPeptide FragmentsPlasmidsConceptsDNA polymerase IOverproducing strainPolymerase IGene fusion techniquesLarge proteolytic fragmentCellular proteinsLac promoterGene fragmentsProtein structurePhage lambdaLeftward promoterEscherichia coliCarboxyl terminalPolymerase fragmentProteolytic fragmentsKlenow fragmentPromoterPlasmidPurification procedureFragmentsOverproductionExpressionI. MoreoverMechanistic studiesCloning
1976
polA6, a mutation affecting the DNA binding capacity of DNA polymerase I
Kelly W, Grindley N. polA6, a mutation affecting the DNA binding capacity of DNA polymerase I. Nucleic Acids Research 1976, 3: 2971-2984. PMID: 12497, PMCID: PMC343145, DOI: 10.1093/nar/3.11.2971.Peer-Reviewed Original ResearchMeSH KeywordsAllelesBinding SitesDNA Polymerase IDNA, BacterialDNA-Directed DNA PolymeraseEscherichia coliGenesHydrogen-Ion ConcentrationKineticsMutationProtein Binding