2012
A Dual Interaction between the DNA Damage Response Protein MDC1 and the RAG1 Subunit of the V(D)J Recombinase*
Coster G, Gold A, Chen D, Schatz DG, Goldberg M. A Dual Interaction between the DNA Damage Response Protein MDC1 and the RAG1 Subunit of the V(D)J Recombinase*. Journal Of Biological Chemistry 2012, 287: 36488-36498. PMID: 22942284, PMCID: PMC3476314, DOI: 10.1074/jbc.m112.402487.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid MotifsBRCA1 ProteinCell Cycle ProteinsCell Line, TumorHistonesHomeodomain ProteinsHumansModels, BiologicalNuclear ProteinsPeptide MappingPhosphorylationProtein Structure, TertiaryRepetitive Sequences, Amino AcidTrans-ActivatorsVDJ RecombinasesConceptsDNA double-strand breaksDNA damage responseTandem BRCA1 C-terminal (BRCT) domainsC-terminusSpecific DNA double-strand breaksBRCA1 C-terminal domainC-terminal domainThreonine-rich repeatsDouble-strand breaksRAG1 subunitRAG recombinaseRAG2 proteinsDDR proteinsDamage responseRegulatory signalsBinding interfaceBreak siteHistone H2AXRAG activityRich repeatsNon-core regionsMDC1RAG1PhosphorylationSubsequent signal amplification
2009
Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis
Yin FF, Bailey S, Innis CA, Ciubotaru M, Kamtekar S, Steitz TA, Schatz DG. Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis. Nature Structural & Molecular Biology 2009, 16: 499-508. PMID: 19396172, PMCID: PMC2715281, DOI: 10.1038/nsmb.1593.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsBase SequenceChromosome PairingCrystallography, X-RayDNAFluorescence Resonance Energy TransferHomeodomain ProteinsMiceModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiarySolutionsStatic Electricity
2003
Regulation of RAG1/RAG2‐mediated transposition by GTP and the C‐terminal region of RAG2
Tsai C, Schatz DG. Regulation of RAG1/RAG2‐mediated transposition by GTP and the C‐terminal region of RAG2. The EMBO Journal 2003, 22: 1922-1930. PMID: 12682024, PMCID: PMC154477, DOI: 10.1093/emboj/cdg185.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCalciumDNADNA-Binding ProteinsGuanosine TriphosphateHomeodomain ProteinsMolecular StructureProtein Structure, TertiaryRecombination, GeneticConceptsFull-length RAG2RAG2 proteinsRegulatory mechanismsC-terminal regionRAG proteinsHybrid joint formationDNA recognitionDNA transpositionCleavage functionChromosomal translocationsGTPUnknown mechanismRAG2ProteinTarget DNAPhysiological concentrationsRegulationJoint formationRAGRAG1MechanismTranslocationDNAGuanineTransposition
2001
Identification of Basic Residues in RAG2 Critical for DNA Binding by the RAG1-RAG2 Complex
Fugmann S, Schatz D. Identification of Basic Residues in RAG2 Critical for DNA Binding by the RAG1-RAG2 Complex. Molecular Cell 2001, 8: 899-910. PMID: 11684024, DOI: 10.1016/s1097-2765(01)00352-5.Peer-Reviewed Original ResearchConceptsDNA bindingRAG2 proteinsCognate DNA target sequenceDNA target sequencesResidue mutantsMolecular roleBasic residuesDNA cleavageTarget sequenceRAG1Biochemical analysisRAG2BindingCentral roleProteinRecombinationResiduesDirect involvementEssential componentComplexesMutantsCleavage reactionIdentificationRoleSequence