2015
Spatio-temporal regulation of RAG2 following genotoxic stress
Rodgers W, Byrum JN, Sapkota H, Rahman NS, Cail RC, Zhao S, Schatz DG, Rodgers KK. Spatio-temporal regulation of RAG2 following genotoxic stress. DNA Repair 2015, 27: 19-27. PMID: 25625798, PMCID: PMC4336829, DOI: 10.1016/j.dnarep.2014.12.008.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAtaxia Telangiectasia Mutated ProteinsCell NucleusCells, CulturedCentrosomeDNADNA Breaks, Double-StrandedDNA RepairDNA-Binding ProteinsGene Knockdown TechniquesHumansMicroscopy, FluorescenceMutationNuclear ProteinsPrecursor Cells, B-LymphoidRadiation, IonizingSubcellular FractionsVDJ RecombinasesConceptsDNA double-strand breaksGenotoxic stressorsCellular responsesFormation of DSBsLymphocyte antigen receptor genesDNA DSBsSpatio-temporal regulationInhibition of ATMDNA damaging agentsSubcellular fractionation approachDouble-strand breaksAntigen receptor genesNuclear Rag2Genotoxic stressRAG complexDNA repairIncorrect repairDamaging agentsStrand breaksNovel mechanismRAG2Receptor geneCentrosomesFractionation approachSubstantial enrichment
2013
Peripheral subnuclear positioning suppresses Tcrb recombination and segregates Tcrb alleles from RAG2
Chan EA, Teng G, Corbett E, Choudhury KR, Bassing CH, Schatz DG, Krangel MS. Peripheral subnuclear positioning suppresses Tcrb recombination and segregates Tcrb alleles from RAG2. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: e4628-e4637. PMID: 24218622, PMCID: PMC3845165, DOI: 10.1073/pnas.1310846110.Peer-Reviewed Original ResearchConceptsTcrb allelesNuclear peripheryNuclear laminaDNA repair protein 53BP1RNA polymerase IIGene 2 proteinHistone H3K4 trimethylationPericentromeric heterochromatinPolymerase IIH3K4 trimethylationRAG proteinsProtein 53BP1Subnuclear distributionRecombination eventsAllelic exclusionDouble-negative thymocytesT-cell receptor βHigher-Order Looping and Nuclear Organization of Tcra Facilitate Targeted RAG Cleavage and Regulated Rearrangement in Recombination Centers
Chaumeil J, Micsinai M, Ntziachristos P, Deriano L, Wang J, Ji Y, Nora EP, Rodesch MJ, Jeddeloh JA, Aifantis I, Kluger Y, Schatz DG, Skok JA. Higher-Order Looping and Nuclear Organization of Tcra Facilitate Targeted RAG Cleavage and Regulated Rearrangement in Recombination Centers. Cell Reports 2013, 3: 359-370. PMID: 23416051, PMCID: PMC3664546, DOI: 10.1016/j.celrep.2013.01.024.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAnimalsAtaxia Telangiectasia Mutated ProteinsCell Cycle ProteinsCell NucleusDNA DamageDNA-Binding ProteinsGenetic LociGenomic InstabilityHistonesHomeodomain ProteinsMiceMice, Inbred C57BLMice, Inbred CBAMice, KnockoutProtein Serine-Threonine KinasesReceptors, Antigen, T-Cell, alpha-betaTumor Suppressor ProteinsV(D)J RecombinationConceptsAntigen receptor lociRegulated rearrangementsGenome stabilityNuclear organizationRAG cleavageRAG recombinaseNuclear accessibilityRAG bindingCellular transformationΑ locusRecombination eventsReceptor locusDiverse arrayCell receptorLociLoop formationTight controlRegulationCleavageFocal bindingGenetic anomaliesBindingKey determinantRearrangementTranscription
2001
Location, location, location: the cell biology of immunoglobulin allelic control
Hesslein D, Fields P, Schatz D. Location, location, location: the cell biology of immunoglobulin allelic control. Nature Immunology 2001, 2: 825-826. PMID: 11526394, DOI: 10.1038/ni0901-825.Peer-Reviewed Original Research
1997
A Basic Motif in the N-Terminal Region of RAG1 Enhances V(D)J Recombination Activity
McMahan C, Difilippantonio M, Rao N, Spanopoulou E, Schatz D. A Basic Motif in the N-Terminal Region of RAG1 Enhances V(D)J Recombination Activity. Molecular And Cellular Biology 1997, 17: 4544-4552. PMID: 9234712, PMCID: PMC232308, DOI: 10.1128/mcb.17.8.4544.Peer-Reviewed Original ResearchConceptsBasic amino acid motifN-terminal regionSite-specific DNA recognitionRecombination activityCell-specific componentsComponent gene segmentsExtrachromosomal recombination substratesAmino acid motifsAmino acids 216Site-specific recombination reactionAntigen receptor genesEvolutionary conservationNuclear transportRAG2 proteinsRAG1 proteinRecombination functionsRecombination substratesDeletion analysisDNA recognitionEnzymatic machineryAcid motifFurther mutagenesisSRP-1N-terminusRAG1Definition of a large region of RAG1 that is important for coimmunoprecipitation of RAG2.
McMahan CJ, Sadofsky MJ, Schatz DG. Definition of a large region of RAG1 that is important for coimmunoprecipitation of RAG2. The Journal Of Immunology 1997, 158: 2202-10. PMID: 9036966, DOI: 10.4049/jimmunol.158.5.2202.Peer-Reviewed Original Research
1995
rag-1 and rag-2 Are Components of a High-Molecular-Weight Complex, and Association of rag-2 with This Complex Is rag-1 Dependent
Leu T, Schatz D. rag-1 and rag-2 Are Components of a High-Molecular-Weight Complex, and Association of rag-2 with This Complex Is rag-1 Dependent. Molecular And Cellular Biology 1995, 15: 5657-5670. PMID: 7565717, PMCID: PMC230816, DOI: 10.1128/mcb.15.10.5657.Peer-Reviewed Original ResearchConceptsRAG-2RAG-1RAG-2 proteinRAG proteinsSubcellular localizationBiological functionsIntracellular complexesWeight complexesLymphocyte developmentSized complexesBiochemical propertiesProteinCell linesSame complexHigh salt concentrationsSynergistic functionImmunological reagentsNuclear structureComplexesCoimmunoprecipitationHigh-MolecularMore moleculesHigh levelsRecombinationSalt concentration