2001
A DNA Polymerase β Mutator Mutant with Reduced Nucleotide Discrimination and Increased Protein Stability † , ‡
Shah A, Conn D, Li S, Capaldi A, Jäger J, Sweasy J. A DNA Polymerase β Mutator Mutant with Reduced Nucleotide Discrimination and Increased Protein Stability † , ‡. Biochemistry 2001, 40: 11372-11381. PMID: 11560485, DOI: 10.1021/bi010755y.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionBase SequenceDeoxyribonucleotidesDNA Mutational AnalysisDNA Polymerase betaDNA, BacterialEnzyme StabilityEscherichia coliFrameshift MutationGene LibraryGenotypeHot TemperatureKineticsModels, ChemicalModels, MolecularMolecular Sequence DataMutationNucleic Acid ConformationPoint MutationProtein ConformationProtein DenaturationSimplexvirusSubstrate SpecificityThermodynamicsThymidine KinaseUreaConceptsNucleotide discriminationPol betaIncreased Protein StabilityVivo genetic screenHydrophobic amino acid residuesDeoxynucleoside triphosphate substratesProtein conformational changesAmino acid residuesC-terminal portionWild-type pol betaDNA synthesis fidelityPhosphodiester bond formationGenetic screenDNA polymerase betaSubstrate discriminationMutator mutantsGround-state bindingHigh mutation frequencyPolymerase structureProtein stabilityMutant enzymesStructural basisTransient-state kinetic methodsAcid residuesMutator activityY265H Mutator Mutant of DNA Polymerase β PROPER GEOMETRIC ALIGNMENT IS CRITICAL FOR FIDELITY*
Shah A, Li S, Anderson K, Sweasy J. Y265H Mutator Mutant of DNA Polymerase β PROPER GEOMETRIC ALIGNMENT IS CRITICAL FOR FIDELITY*. Journal Of Biological Chemistry 2001, 276: 10824-10831. PMID: 11154692, DOI: 10.1074/jbc.m008680200.Peer-Reviewed Original ResearchConceptsDNA polymerase betaPolymerase betaVivo genetic screenWild-type proteinWild-type enzymeActive site residuesGenetic screenTyr-265Mutant proteinsMutator mutantsPolymerase structureProper geometric alignmentSite residuesProtein conformationNucleotidyl transferForward mutationDNA polymerasePolymerase fidelityDNTP substratesDNA synthesisProteinDeoxynucleoside triphosphatesFirst evidenceTemplate A.Enzyme
1999
Involvement of Phenylalanine 272 of DNA Polymerase Beta in Discriminating between Correct and Incorrect Deoxynucleoside Triphosphates †
Li S, Vaccaro J, Sweasy J. Involvement of Phenylalanine 272 of DNA Polymerase Beta in Discriminating between Correct and Incorrect Deoxynucleoside Triphosphates †. Biochemistry 1999, 38: 4800-4808. PMID: 10200168, DOI: 10.1021/bi9827058.Peer-Reviewed Original ResearchConceptsDNA polymerase betaPolymerase betaWild typeVivo genetic screenWild-type enzymeBase excision repairDeoxynucleoside triphosphatesGenetic screenBase substitution mutationsMutator mutantsGround-state bindingType enzymeExcision repairResidue 272Substitution mutationsIncorrect dNTPMutantsDecreased fidelityFrameshift mutation
1997
A genetic system to identify DNA polymerase β mutator mutants
Washington S, Yoon M, Chagovetz A, Li S, Clairmont C, Preston B, Eckert K, Sweasy J. A genetic system to identify DNA polymerase β mutator mutants. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 1321-1326. PMID: 9037051, PMCID: PMC19789, DOI: 10.1073/pnas.94.4.1321.Peer-Reviewed Original ResearchConceptsMutator mutantsGenetic methodsPol betaDNA synthesisAccurate DNA synthesisDNA repair processesRat pol betaWild-type pol betaEscherichia coli DNA polymerase ISpontaneous mutation frequencyDNA polymerase IAltered fidelityDNA polymerase betaMutant proteinsDNA replicationGenetic systemMammalian cellsGenetic assaysPolymerase IMutantsDNA polymerase mutantsMutator activityPolymerase mutantsBeta enzymePolymerase beta