Featured Publications
Structural insights into the evolution of the RAG recombinase
Liu C, Zhang Y, Liu CC, Schatz DG. Structural insights into the evolution of the RAG recombinase. Nature Reviews Immunology 2021, 22: 353-370. PMID: 34675378, DOI: 10.1038/s41577-021-00628-6.Peer-Reviewed Original ResearchConceptsRAG recombinaseComparative genome analysisGenomes of eukaryotesProtein-DNA complexesSingle amino acid mutationAntigen receptor genesMolecular domesticationRag familyAmino acid mutationsJawed vertebratesVertebrate immunityTransposable elementsEvolutionary adaptationGenome analysisStructural biologyDNA bindingStructural insightsGene 1Acid mutationsCleavage activityRecombinaseReceptor geneStructural evidenceRecombinationAdaptive immunity
2016
Collaboration of RAG2 with RAG1-like proteins during the evolution of V(D)J recombination
Carmona LM, Fugmann SD, Schatz DG. Collaboration of RAG2 with RAG1-like proteins during the evolution of V(D)J recombination. Genes & Development 2016, 30: 909-917. PMID: 27056670, PMCID: PMC4840297, DOI: 10.1101/gad.278432.116.Peer-Reviewed Original ResearchConceptsRecombination-activating gene 1Transib transposaseAbsence of RAG2RAG1/RAG2Antigen receptor genesJawed vertebratesRAG2 proteinsTransposable elementsRAG1 proteinRegulatory featuresDNA substratesGene 1RAG2Receptor geneRecombination activityProteinRecombinationTransposaseAdaptive immunityVertebratesTransposonGenesEvolutionLow levelsOrigin
2015
Chapter 2 The Mechanism of V(D)J Recombination
Little A, Matthews A, Oettinger M, Roth D, Schatz D. Chapter 2 The Mechanism of V(D)J Recombination. 2015, 13-34. DOI: 10.1016/b978-0-12-397933-9.00002-3.ChaptersLymphocyte developmentNonhomologous end-joining pathwayRegulation of recombinationAntigen receptor lociEnd-joining pathwayDNA repair proteinsRecombination-activating gene 1RAG proteinsDNA breaksRecombinase machineryFunctional antigen receptorEnd processingReceptor locusGenetic instabilityGene 1Recombinase activityChromosomal translocationsDNA cleavageProtein 1Diverse repertoireRepair stepsBox protein 1Antigen receptorHigh mobility group box protein 1Recombination
2007
The Beyond 12/23 Restriction Is Imposed at the Nicking and Pairing Steps of DNA Cleavage during V(D)J Recombination
Drejer-Teel AH, Fugmann SD, Schatz DG. The Beyond 12/23 Restriction Is Imposed at the Nicking and Pairing Steps of DNA Cleavage during V(D)J Recombination. Molecular And Cellular Biology 2007, 27: 6288-6299. PMID: 17636023, PMCID: PMC2099602, DOI: 10.1128/mcb.00835-07.Peer-Reviewed Original ResearchConceptsRecombination signal sequencesDNA cleavageGene segmentsDNA cleavage stepRecombination-activating gene 1Dbeta gene segmentVariable region exonsJbeta gene segmentsRAG proteinsDNA elementsSignal sequenceDirect VbetaRegion exonsGene 1Oligonucleotide substratesLocus sequenceDistinct combinationsProteinRecombinationCleavageNickingCleavage stepSequenceDifferent stepsExons
2004
New concepts in the regulation of an ancient reaction: transposition by RAG1/RAG2
Chatterji M, Tsai C, Schatz DG. New concepts in the regulation of an ancient reaction: transposition by RAG1/RAG2. Immunological Reviews 2004, 200: 261-271. PMID: 15242411, DOI: 10.1111/j.0105-2896.2004.00167.x.Peer-Reviewed Original ResearchConceptsRAG proteinsRecombination-activating gene 1Transposition activityAntigen receptor lociDNA double-stand breaksRAG1/RAG2Lymphoid-specific factorsDouble-stand breaksEndonuclease activityGene 1Chromosomal translocationsVariety of mechanismsProteinSpecific sitesRAG2Ancient reactionRecombinationRecent studiesGenome
1996
A Zinc-binding Domain Involved in the Dimerization of RAG1
Rodgers K, Bu Z, Fleming K, Schatz D, Engelman D, Coleman J. A Zinc-binding Domain Involved in the Dimerization of RAG1. Journal Of Molecular Biology 1996, 260: 70-84. PMID: 8676393, DOI: 10.1006/jmbi.1996.0382.Peer-Reviewed Original ResearchConceptsRecombination-activating gene 1Zinc-binding motifDimerization domainZinc fingerProtein-protein interactionsLymphoid-specific genesN-terminal thirdZinc finger sequencesAmino acid residuesC3HC4 motifRAG1 sequencesRAG1 proteinTerminal domainHomodimer formationAcid residuesBiophysical techniquesGene 1Energetics of associationMonomeric subunitsMotifProteinFinger sequencesSequenceC3HC4Zinc ions
1995
A modified tetracycline-regulated system provides autoregulatory, inducible gene expression in cultured cells and transgenic mice.
Shockett P, Difilippantonio M, Hellman N, Schatz DG. A modified tetracycline-regulated system provides autoregulatory, inducible gene expression in cultured cells and transgenic mice. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 6522-6526. PMID: 7604026, PMCID: PMC41550, DOI: 10.1073/pnas.92.14.6522.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsBlotting, WesternCells, CulturedDNA NucleotidyltransferasesGene Expression RegulationHerpes Simplex Virus Protein Vmw65MiceMice, TransgenicOpen Reading FramesPlasmidsRecombinant Fusion ProteinsRepressor ProteinsRestriction MappingRNA, MessengerSequence DeletionTetracyclineTrans-ActivatorsTransfectionVDJ RecombinasesConceptsInducible gene expressionGene expressionTetracycline-regulated gene expressionTranscriptional activation domainCultured cellsTetracycline-regulated systemTransgenic miceExpression of tTAAutoregulatory systemActivation domainTTA geneInducible promoterTetracycline repressorInducible expressionFusion proteinTransactivator proteinConstitutive expressionTransgenic animalsGene 1Induced levelsRecombination activityMost tissuesConstitutive systemProteinCell lines