2008
Fingers-Closing and Other Rapid Conformational Changes in DNA Polymerase I (Klenow Fragment) and Their Role in Nucleotide Selectivity
Joyce CM, Potapova O, DeLucia AM, Huang X, Basu VP, Grindley ND. Fingers-Closing and Other Rapid Conformational Changes in DNA Polymerase I (Klenow Fragment) and Their Role in Nucleotide Selectivity. Biochemistry 2008, 47: 6103-6116. PMID: 18473481, DOI: 10.1021/bi7021848.Peer-Reviewed Original Research
2003
Interaction of DNA Polymerase I (Klenow Fragment) with the Single-Stranded Template beyond the Site of Synthesis †
Turner R, Grindley N, Joyce C. Interaction of DNA Polymerase I (Klenow Fragment) with the Single-Stranded Template beyond the Site of Synthesis †. Biochemistry 2003, 42: 2373-2385. PMID: 12600204, DOI: 10.1021/bi026566c.Peer-Reviewed Original Research
2002
Discrimination against purine–pyrimidine mispairs in the polymerase active site of DNA polymerase I: A structural explanation
Minnick D, Liu L, Grindley N, Kunkel T, Joyce C. Discrimination against purine–pyrimidine mispairs in the polymerase active site of DNA polymerase I: A structural explanation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 1194-1199. PMID: 11830658, PMCID: PMC122166, DOI: 10.1073/pnas.032457899.Peer-Reviewed Original Research
2001
The basis of asymmetry in IS2 transposition
Lewis L, Gadura N, Greene M, Saby R, Grindley N. The basis of asymmetry in IS2 transposition. Molecular Microbiology 2001, 42: 887-901. PMID: 11737634, DOI: 10.1046/j.1365-2958.2001.02662.x.Peer-Reviewed Original ResearchContacts between the 5′ Nuclease of DNA Polymerase I and Its DNA Substrate*
Xu Y, Potapova O, Leschziner A, Grindley N, Joyce C. Contacts between the 5′ Nuclease of DNA Polymerase I and Its DNA Substrate*. Journal Of Biological Chemistry 2001, 276: 30167-30177. PMID: 11349126, DOI: 10.1074/jbc.m100985200.Peer-Reviewed Original ResearchMeSH KeywordsArginineBase SequenceBinding SitesCircular DichroismDNADNA Polymerase IDNA RepairEscherichia coliKineticsLysineModels, ChemicalModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationOrganophosphorus CompoundsPhosphatesProtein BindingProtein Structure, TertiarySubstrate SpecificityTemperatureTime FactorsConceptsDNA substratesDNA polymerase INuclease domainCleavage siteBasic residuesPolymerase IDuplex DNANuclease cleavagePhosphate ethylation interferenceDNA-binding regionActive site regionDNA replicationOne-half turnBacteriophage T5Eukaryotic nucleasesSubstrate bindingAbasic DNAEthylation interferenceDuplex portionHelical archNucleaseSite regionEscherichia coliMethylphosphonate substitutionsPrimer strand
1995
Deoxynucleoside Triphosphate and Pyrophosphate Binding Sites in the Catalytically Competent Ternary Complex for the Polymerase Reaction Catalyzed by DNA Polymerase I (Klenow Fragment) (∗)
Astatke M, Grindley N, Joyce C. Deoxynucleoside Triphosphate and Pyrophosphate Binding Sites in the Catalytically Competent Ternary Complex for the Polymerase Reaction Catalyzed by DNA Polymerase I (Klenow Fragment) (∗). Journal Of Biological Chemistry 1995, 270: 1945-1954. PMID: 7829532, DOI: 10.1074/jbc.270.4.1945.Peer-Reviewed Original ResearchAmino Acid SequenceBacteriaBase SequenceBinding SitesConserved SequenceDeoxyribonucleotidesDiphosphatesDNA Polymerase IDNA PrimersKineticsMacromolecular SubstancesModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedOligodeoxyribonucleotidesPoint MutationPolymerase Chain ReactionProtein Structure, SecondarySaccharomyces cerevisiaeSequence Homology, Amino Acid
1993
Protein‐protein interactions directing resolvase site‐specific recombination: a structure‐function analysis.
Hughes R, Rice P, Steitz T, Grindley N. Protein‐protein interactions directing resolvase site‐specific recombination: a structure‐function analysis. The EMBO Journal 1993, 12: 1447-1458. PMID: 8385604, PMCID: PMC413356, DOI: 10.1002/j.1460-2075.1993.tb05788.x.Peer-Reviewed Original Research
1991
The 3′‐5′ exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction.
Derbyshire V, Grindley N, Joyce C. The 3′‐5′ exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. The EMBO Journal 1991, 10: 17-24. PMID: 1989882, PMCID: PMC452606, DOI: 10.1002/j.1460-2075.1991.tb07916.x.Peer-Reviewed Original ResearchConceptsActive siteMetal ionsEnzyme-bound metal ionSide chainsExonuclease reactionDivalent metal ionsAmino acid side chainsCarboxylate side chainAcid side chainsHydroxide ionMetal ligandsNucleophilic attackIonsTerminal phosphodiester bondPhosphodiester bondReactionExonuclease active siteActivity resultsKlenow fragmentDuplex DNA substratesCatalysisChainCarboxylateTerminal baseSubstrate