2017
DNA polymerase beta participates in DNA End-joining
Ray S, Breuer G, DeVeaux M, Zelterman D, Bindra R, Sweasy JB. DNA polymerase beta participates in DNA End-joining. Nucleic Acids Research 2017, 46: 242-255. PMID: 29161447, PMCID: PMC5758893, DOI: 10.1093/nar/gkx1147.Peer-Reviewed Original ResearchConceptsDouble-strand breaksAlternative NHEJHomologous recombinationDNA polymerasePol βX-family DNA polymerasesFamily DNA polymerasesDNA polymerase betaDNA pol βDeleterious lesionsDNA endsGenomic instabilityNHEJ pathwayDNA proteinProcessing enzymesDefective repairCellular sensitivityCell deathStrand breaksPolymerase betaSubunit inhibitorPolymeraseSmall deletionsMechanistic insightsNHEJ
2002
Crystal Structures of the Bacillus stearothermophilus CCA-Adding Enzyme and Its Complexes with ATP or CTP
Li F, Xiong Y, Wang J, Cho HD, Tomita K, Weiner AM, Steitz TA. Crystal Structures of the Bacillus stearothermophilus CCA-Adding Enzyme and Its Complexes with ATP or CTP. Cell 2002, 111: 815-824. PMID: 12526808, DOI: 10.1016/s0092-8674(02)01115-7.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceCrystallography, X-RayCytidine TriphosphateDimerizationDNA Polymerase betaGeobacillus stearothermophilusModels, MolecularMolecular Sequence DataProtein FoldingProtein Structure, TertiaryRNA NucleotidyltransferasesSequence Homology, Amino AcidConceptsCCA-adding enzymeResolution crystal structureDNA polymerase betaImmature tRNAsNew proteinsBase specificityNucleic acid templateBacillus stearothermophilusPalm domainPolymerase betaIncoming ATPTRNAATPTerminusSubunitsCrystal structureActive siteAdditional structural featuresEnzymeCTPStructural featuresComplexesImportant componentTailDomainThreonine 79 Is a Hinge Residue That Governs the Fidelity of DNA Polymerase β by Helping to Position the DNA within the Active Site*
Maitra M, Gudzelak A, Li SX, Matsumoto Y, Eckert KA, Jager J, Sweasy JB. Threonine 79 Is a Hinge Residue That Governs the Fidelity of DNA Polymerase β by Helping to Position the DNA within the Active Site*. Journal Of Biological Chemistry 2002, 277: 35550-35560. PMID: 12121998, DOI: 10.1074/jbc.m204953200.Peer-Reviewed Original ResearchConceptsHelix motifPol betaDNA synthesisThr-79Vivo genetic screenAccurate DNA synthesisDifferent amino acid residuesAmino acid residuesWild-type pol betaN-terminal 8DNA polymerase βGenetic screenDNA polymerase betaAntimutator phenotypeDNA substratesIncoming dNTP substrateActive siteWild typeBent DNAHinge residuesAcid residuesDNA templateBeta enzymePolymerase βPolymerase beta
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
The Tyr-265-to-Cys mutator mutant of DNA polymerase β induces a mutator phenotype in mouse LN12 cells
Clairmont C, Narayanan L, Sun K, Glazer P, Sweasy J. The Tyr-265-to-Cys mutator mutant of DNA polymerase β induces a mutator phenotype in mouse LN12 cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 9580-9585. PMID: 10449735, PMCID: PMC22251, DOI: 10.1073/pnas.96.17.9580.Peer-Reviewed Original ResearchConceptsMutator mutantsDNA polymerase betaTyr-265Mutator phenotypePolymerase betaWild-type DNA polymerase betaWild-type DNA polymeraseWild-type proteinBase excision repairRat DNA polymerase betaSpontaneous mutation frequencyDNA polymerase βDNA polymerase IMammalian cellsMutator polymeraseComplementation systemBeta mutantsExcision repairPolymerase IMutantsMutator activityGenetic instabilityHuman cellsPolymerase βEscherichia coliInvolvement 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
1990
Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain.
Kumar A, Widen S, Williams K, Kedar P, Karpel R, Wilson S. Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain. Journal Of Biological Chemistry 1990, 265: 2124-2131. PMID: 2404980, DOI: 10.1016/s0021-9258(19)39949-1.Peer-Reviewed Original ResearchConceptsNH2-terminal domainDNA polymerase betaLarge-scale overproductionPolymerase betaMammalian DNA polymerase betaCOOH-terminal domainProtease-sensitive regionNucleic acidsProteolysis experimentsRat proteinRecombinant proteinsPolypeptide chainDNA polymerase activityIntact proteinEscherichia coliAmino acidsTryptic peptidesDNA polymeraseDomain structureProteinPolymerase activityDomainPolymeraseAcidDNA
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