2001
Autostimulation of the Epstein-Barr Virus BRLF1 Promoter Is Mediated through Consensus Sp1 and Sp3 Binding Sites
Ragoczy T, Miller G. Autostimulation of the Epstein-Barr Virus BRLF1 Promoter Is Mediated through Consensus Sp1 and Sp3 Binding Sites. Journal Of Virology 2001, 75: 5240-5251. PMID: 11333906, PMCID: PMC114930, DOI: 10.1128/jvi.75.11.5240-5251.2001.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBinding SitesB-LymphocytesCell Line, TransformedDNA-Binding ProteinsGene DeletionGene Expression Regulation, ViralHerpesvirus 4, HumanHeterotrimeric GTP-Binding ProteinsHumansImmediate-Early ProteinsMolecular Sequence DataMutagenesis, Site-DirectedPromoter Regions, GeneticProtein BindingReceptors, Cell SurfaceSp1 Transcription FactorSp3 Transcription FactorTrans-ActivatorsTranscription FactorsViral ProteinsVirus ActivationConceptsSp1/Sp3 siteLytic cycleSp3 transcription factorsBinding of Sp1Transcriptional start siteSite-directed mutagenesisGel shift analysisBRLF1 promoterReporter-based assaysEpstein–Barr virus Rta proteinCellular Sp1Own geneConsensus Sp1Transcriptional activationCellular proteinsTranscription factorsStart siteDNA bindingOwn expressionMutagenesis studiesRta proteinSp1Reporter activityTranscription factor Zif268B cells
1999
Amino Acid Substitutions Reveal Distinct Functions of Serine 186 of the ZEBRA Protein in Activation of Early Lytic Cycle Genes and Synergy with the Epstein-Barr Virus R Transactivator
Francis A, Ragoczy T, Gradoville L, Heston L, El-Guindy A, Endo Y, Miller G. Amino Acid Substitutions Reveal Distinct Functions of Serine 186 of the ZEBRA Protein in Activation of Early Lytic Cycle Genes and Synergy with the Epstein-Barr Virus R Transactivator. Journal Of Virology 1999, 73: 4543-4551. PMID: 10233912, PMCID: PMC112494, DOI: 10.1128/jvi.73.6.4543-4551.1999.Peer-Reviewed Original ResearchConceptsLytic cycle genesLatent virusZEBRA proteinOverexpression of RtaEpstein-Barr virusLatent EBV genomeBRLF1 expressionEarly lytic cycle genesAmino acid substitutionsEBV genomeBRLF1BRLF1 promoterCycle genesAcid substitutionsVirusEpstein-Barr virus R transactivatorSerine 186Distinct phenotypesLytic life cycleR transactivatorActivationDifferent amino acid substitutionsResponse elementS186ExpressionKaposi’s Sarcoma-Associated Herpesvirus Encodes a bZIP Protein with Homology to BZLF1 of Epstein-Barr Virus
Lin S, Robinson D, Miller G, Kung H. Kaposi’s Sarcoma-Associated Herpesvirus Encodes a bZIP Protein with Homology to BZLF1 of Epstein-Barr Virus. Journal Of Virology 1999, 73: 1909-1917. PMID: 9971770, PMCID: PMC104432, DOI: 10.1128/jvi.73.3.1909-1917.1999.Peer-Reviewed Original Research
1998
The Epstein-Barr Virus Rta Protein Activates Lytic Cycle Genes and Can Disrupt Latency in B Lymphocytes
Ragoczy T, Heston L, Miller G. The Epstein-Barr Virus Rta Protein Activates Lytic Cycle Genes and Can Disrupt Latency in B Lymphocytes. Journal Of Virology 1998, 72: 7978-7984. PMID: 9733836, PMCID: PMC110133, DOI: 10.1128/jvi.72.10.7978-7984.1998.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceB-LymphocytesCell LineChloramphenicol O-AcetyltransferaseDNA PrimersDNA ReplicationDNA-Binding ProteinsGene Expression Regulation, ViralHerpesvirus 4, HumanHumansImmediate-Early ProteinsPromoter Regions, GeneticTrans-ActivatorsTranscription FactorsViral ProteinsVirus LatencyConceptsEpstein-Barr virusLytic cycle genesB lymphocytesEpstein–Barr virus Rta proteinEpithelial cellsLytic cycleDisruption of latencyViral lytic cycleB cell linesEBV entryImmediate early viral genesBZLF1LymphocytesCycle genesExpression of RTARTA functionBRLF1Rta proteinDownstream targetsViral genesViral DNA replicationExpressionCells
1997
The Locus of Epstein–Barr Virus Terminal Repeat Processing Is Bound with Enhanced Affinity by Sp1 and Sp3
Spain T, Sun R, Miller G. The Locus of Epstein–Barr Virus Terminal Repeat Processing Is Bound with Enhanced Affinity by Sp1 and Sp3. Virology 1997, 237: 137-147. PMID: 9344916, DOI: 10.1006/viro.1997.8770.Peer-Reviewed Original ResearchConceptsRecombination eventsRepeat binding proteinMinimal binding siteAntibody supershift assaysRepeat processingSp1 sitesCellular proteinsLarge internal repeatRecombinogenic regionsInternal repeatsSp1Supershift assaysRecombinant proteinsTerminal repeatBinding proteinLytic cycle inductionEBV lytic cycle inductionCycle inductionProteinAffinity of bindingBinding sitesRepeatsSite 1DNASp3