2005
A specific subdomain in φ29 DNA polymerase confers both processivity and strand-displacement capacity
Rodríguez I, Lázaro JM, Blanco L, Kamtekar S, Berman AJ, Wang J, Steitz TA, Salas M, de Vega M. A specific subdomain in φ29 DNA polymerase confers both processivity and strand-displacement capacity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 6407-6412. PMID: 15845765, PMCID: PMC1088371, DOI: 10.1073/pnas.0500597102.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacteriophage T4DNADNA PrimersDNA ReplicationDNA-Directed DNA PolymeraseElectrophoretic Mobility Shift AssayExodeoxyribonucleasesModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein ConformationProtein Structure, TertiarySequence AlignmentTemplates, GeneticConceptsDNA polymerasePhi29 DNA polymeraseProtein-primed DNA polymerasesStrand-displacement capacityMutant DNA polymerasesΦ29 DNA polymeraseRecent crystallographic studiesDNA binding capacityAsp-398Deletion mutantsStructural insightsSpecific insertionProcessivityPolymeraseStrand displacementFunctional roleAmino acidsPalm subdomainSpecific subdomainsBiochemical analysisDNA synthesisCritical roleRegion 2Crystallographic studiesIntrinsic capacity
2004
Insights into Strand Displacement and Processivity from the Crystal Structure of the Protein-Primed DNA Polymerase of Bacteriophage φ29
Kamtekar S, Berman AJ, Wang J, Lázaro JM, de Vega M, Blanco L, Salas M, Steitz TA. Insights into Strand Displacement and Processivity from the Crystal Structure of the Protein-Primed DNA Polymerase of Bacteriophage φ29. Molecular Cell 2004, 16: 609-618. PMID: 15546620, DOI: 10.1016/j.molcel.2004.10.019.Peer-Reviewed Original ResearchConceptsDNA polymerasePhi29 DNA polymeraseT7 RNA polymeraseB-family polymerasesSpecific serinePriming proteinPolymerase active sitePhage phi29RNA polymerasePhage genomeSpecificity loopNontemplate strandStrand displacement activityFirst nucleotideHomology modelingSequence insertionHigh processivityProtein primerB familyPolymeraseDuplex DNATemplate DNAProcessivityProteinDNAPre-Steady-State Kinetics of RB69 DNA Polymerase and Its Exo Domain Mutants: Effect of pH and Thiophosphoryl Linkages on 3‘−5‘ Exonuclease Activity †
Wang C, Zakharova E, Li J, Joyce C, Wang J, Konigsberg W. Pre-Steady-State Kinetics of RB69 DNA Polymerase and Its Exo Domain Mutants: Effect of pH and Thiophosphoryl Linkages on 3‘−5‘ Exonuclease Activity †. Biochemistry 2004, 43: 3853-3861. PMID: 15049692, DOI: 10.1021/bi0302292.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SubstitutionBacteriophage T4Base Pair MismatchDNA Polymerase IDNA-Directed DNA PolymeraseEnzyme ActivationExodeoxyribonucleasesGlutamineHydrogen-Ion ConcentrationKineticsMutagenesis, Site-DirectedPhosphatesPhosphorylationProtein Structure, TertiaryRNA EditingSubstrate SpecificityThionucleotidesT-PhagesViral ProteinsConceptsRate-determining stepDivalent metal ionsPH-activity profileB family replicative DNA polymerasesChemical stepMetal ionsSingle-turnover conditionsWild-type enzymeEffects of pHKlenow fragmentB-family DNA polymerasesFamily DNA polymerasesState kineticsDNA polymeraseThree-dimensional structureDomain mutantsExonuclease reactionExonuclease activityPhosphorothioate linkagesPhi29 DNA polymeraseElemental effectsReplicative DNA polymerasesRepair DNA polymerasesExo activityCatalysis