2004
B cell–specific loss of histone 3 lysine 9 methylation in the VH locus depends on Pax5
Johnson K, Pflugh DL, Yu D, Hesslein DG, Lin KI, Bothwell AL, Thomas-Tikhonenko A, Schatz DG, Calame K. B cell–specific loss of histone 3 lysine 9 methylation in the VH locus depends on Pax5. Nature Immunology 2004, 5: 853-861. PMID: 15258579, PMCID: PMC1635547, DOI: 10.1038/ni1099.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceB-LymphocytesCell LineageCells, CulturedDNA-Binding ProteinsFlow CytometryGene Rearrangement, B-LymphocyteHematopoietic Stem CellsHistonesImmunoglobulin Heavy ChainsImmunoglobulin Variable RegionLysineMethylationMiceModels, ImmunologicalMolecular Sequence DataPAX5 Transcription FactorPrecipitin TestsReverse Transcriptase Polymerase Chain ReactionTranscription FactorsConceptsH3-K9 methylationDJH recombinationVH locusHistone 3 lysine 9 methylationLysine 9 methylationFunction of Pax5Non-B lineage cellsB cell-specific lossB cell commitmentHistone exchangeInactive chromatinLysine 9Histone H3Transcription factorsCell commitmentCell-specific lossInhibitory modificationMethylationLineage cellsLociPAX5B cellsHeavy chain rearrangementRecombinationChain rearrangement
1997
RAG1 and RAG2 Form a Stable Postcleavage Synaptic Complex with DNA Containing Signal Ends in V(D)J Recombination
Agrawal A, Schatz D. RAG1 and RAG2 Form a Stable Postcleavage Synaptic Complex with DNA Containing Signal Ends in V(D)J Recombination. Cell 1997, 89: 43-53. PMID: 9094713, DOI: 10.1016/s0092-8674(00)80181-6.Peer-Reviewed Original ResearchConceptsSignal endsRecombination signalsDNA-dependent protein kinaseProtein-DNA complexesSynaptic complexHMG-2 proteinStable complexesDNA adjacentProtein kinaseProteins RAG1Immunoprecipitation experimentsMobility shiftNuclease sensitivityHMG-1Cleavage systemRAG1RAG2RecombinationComplexesVivo observationsKinaseProteinImportant stepCleavageDefinition 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