2022
Human WDR5 promotes breast cancer growth and metastasis via KMT2-independent translation regulation
Cai WL, Chen JF, Chen H, Wingrove E, Kurley SJ, Chan LH, Zhang M, Arnal-Estape A, Zhao M, Balabaki A, Li W, Yu X, Krop ED, Dou Y, Liu Y, Jin J, Westbrook TF, Nguyen DX, Yan Q. Human WDR5 promotes breast cancer growth and metastasis via KMT2-independent translation regulation. ELife 2022, 11: e78163. PMID: 36043466, PMCID: PMC9584608, DOI: 10.7554/elife.78163.Peer-Reviewed Original ResearchConceptsBreast cancer cellsMetastatic breast cancerBreast cancerRibosomal gene expressionCancer cellsKnockdown of WDR5Vivo genetic screenReversible epigenetic mechanismsGenetic screenTranslation regulationTriple-negative breast cancerEpigenetic regulatorsEpigenetic mechanismsBreast cancer growthCancer-related deathTranslation efficiencyWDR5Novel therapeutic strategiesTranslation rateGene expressionCell growthAdvanced diseaseEffective therapyMetastatic capabilityPotent suppression
2002
Threonine 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
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
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