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
1998
Architecture of the γδ Resolvase Synaptosome Oriented Heterodimers Identify Interactions Essential for Synapsis and Recombination
Murley L, Grindley N. Architecture of the γδ Resolvase Synaptosome Oriented Heterodimers Identify Interactions Essential for Synapsis and Recombination. Cell 1998, 95: 553-562. PMID: 9827807, DOI: 10.1016/s0092-8674(00)81622-0.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
1990
Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli.
Polesky A, Steitz T, Grindley N, Joyce C. Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli. Journal Of Biological Chemistry 1990, 265: 14579-14591. PMID: 2201688, DOI: 10.1016/s0021-9258(18)77342-0.Peer-Reviewed Original ResearchConceptsCluster of residuesIdentification of residuesSite-directed mutagenesisActive site residuesAmino acid residuesFuture mutational studiesImportant active site residuesDNA-binding propertiesActive site regionDNA polymerase IGenetic screenPosition 849Polymerase active siteMutant proteinsDNA substratesMutational studiesPolymerase IBiochemical experimentsSite residuesAcid residuesSite regionEscherichia coliPolymerase activityMutationsPolymerase reaction
1984
Cleavage of the site-specific recombination protein gamma delta resolvase: the smaller of two fragments binds DNA specifically.
Abdel-Meguid S, Grindley N, Templeton N, Steitz T. Cleavage of the site-specific recombination protein gamma delta resolvase: the smaller of two fragments binds DNA specifically. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 2001-2005. PMID: 6326096, PMCID: PMC345424, DOI: 10.1073/pnas.81.7.2001.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 ResearchConceptsDNA polymerase IOverproducing strainPolymerase IGene fusion techniquesLarge proteolytic fragmentCellular proteinsLac promoterGene fragmentsProtein structurePhage lambdaLeftward promoterEscherichia coliCarboxyl terminalPolymerase fragmentProteolytic fragmentsKlenow fragmentPromoterPlasmidPurification procedureFragmentsOverproductionExpressionI. MoreoverMechanistic studiesCloning
1982
Nucleotide sequence of the Escherichia coli polA gene and primary structure of DNA polymerase I.
Joyce C, Kelley W, Grindley N. Nucleotide sequence of the Escherichia coli polA gene and primary structure of DNA polymerase I. Journal Of Biological Chemistry 1982, 257: 1958-1964. PMID: 6276402, DOI: 10.1016/s0021-9258(19)68132-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceDNA Restriction EnzymesEscherichia coliGenesPeptide FragmentsPlasmidsConceptsDNA polymerase IPolymerase INucleotide sequencePolA geneKilobase pair regionProtein chemical dataAmino acid sequenceWild-type alleleResidues 342Sequence comparisonDNA polymerase I.Polymerase moleculesDNA sequencesResidue 323Acid sequencePair regionPolA1 mutationPolymerase I.Primary structureBase pairsType alleleMild proteolysisGenesActive fragmentSequence