2022
Modulation of mRNA 3′-End Processing and Transcription Termination in Virus-Infected Cells
Vijayakumar A, Park A, Steitz JA. Modulation of mRNA 3′-End Processing and Transcription Termination in Virus-Infected Cells. Frontiers In Immunology 2022, 13: 828665. PMID: 35222412, PMCID: PMC8866245, DOI: 10.3389/fimmu.2022.828665.Peer-Reviewed Original Research
2021
SARS-CoV-2 expresses a microRNA-like small RNA able to selectively repress host genes
Pawlica P, Yario TA, White S, Wang J, Moss WN, Hui P, Vinetz JM, Steitz JA. SARS-CoV-2 expresses a microRNA-like small RNA able to selectively repress host genes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2116668118. PMID: 34903581, PMCID: PMC8719879, DOI: 10.1073/pnas.2116668118.Peer-Reviewed Original ResearchConceptsBasic leucine zipper ATF-like transcription factor 2Small RNAsHuman lung-derived cell linesSARS-CoV-2 infectionLung-derived cell linesRNA interference (RNAi) pathwayHost miRNA levelsTranscription factor 2Cellular machineryInterference pathwayDrosha proteinSARS-CoV-2-infected individualsHost genesSevere acute respiratory syndrome coronavirus 2Acute respiratory syndrome coronavirus 2Respiratory syndrome coronavirus 2Host miRNAsPutative targetsSyndrome coronavirus 2SARS-CoV-2MiRNA levelsFactor 2Cell linesNasopharyngeal swabsCoronavirus 2
2018
Two herpesviral noncoding PAN RNAs are functionally homologous but do not associate with common chromatin loci
Withers JB, Li ES, Vallery TK, Yario TA, Steitz JA. Two herpesviral noncoding PAN RNAs are functionally homologous but do not associate with common chromatin loci. PLOS Pathogens 2018, 14: e1007389. PMID: 30383841, PMCID: PMC6233925, DOI: 10.1371/journal.ppat.1007389.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineCell NucleusChromatinGene Expression Regulation, ViralGene Knockdown TechniquesHEK293 CellsHerpesviridaeHerpesviridae InfectionsHerpesvirus 8, HumanHost-Pathogen InteractionsHumansMacaca mulattaRhadinovirusRNA, Long NoncodingRNA, MessengerRNA, NuclearRNA, ViralTumor Virus InfectionsViral ProteinsVirus ReplicationConceptsKaposi's sarcoma-associated herpesvirusPAN RNAPAN RNA expressionGene expressionChromatin lociSarcoma-associated herpesvirusViral mRNAsSpecific chromatin lociNuclear mRNA exportNucleotide sequence conservationAbundant nuclear RNARNA expressionLytic viral gene expressionViral gene expressionMRNA exportRNA associationSequence conservationPolyadenylated transcriptsViral chromatinLoci differHost chromatinRNA functionCell fractionationNuclear RNAProgeny virion release
2015
Proteomics and Transcriptomics of BJAB Cells Expressing the Epstein-Barr Virus Noncoding RNAs EBER1 and EBER2
Pimienta G, Fok V, Haslip M, Nagy M, Takyar S, Steitz JA. Proteomics and Transcriptomics of BJAB Cells Expressing the Epstein-Barr Virus Noncoding RNAs EBER1 and EBER2. PLOS ONE 2015, 10: e0124638. PMID: 26121143, PMCID: PMC4487896, DOI: 10.1371/journal.pone.0124638.Peer-Reviewed Original ResearchConceptsMRNA-seq dataHost cell nucleusBJAB cellsCell proliferationGene expression featuresPro-survival effectsProtein adaptersAlternative splicingMRNA transcriptomeUpregulated proteinsSILAC dataRich elementsAkt activationPI3K-AktBiochemical assaysCell nucleiEBV latencySwitch eventsProteinMaintenance of latencyCell linesVEGFA proteinMechanistic explanationUpregulated oncogenesPIK3AP1
2014
Nuclear Translocation and Regulation of Intranuclear Distribution of Cytoplasmic Poly(A)-Binding Protein Are Distinct Processes Mediated by Two Epstein Barr Virus Proteins
Park R, El-Guindy A, Heston L, Lin SF, Yu KP, Nagy M, Borah S, Delecluse HJ, Steitz J, Miller G. Nuclear Translocation and Regulation of Intranuclear Distribution of Cytoplasmic Poly(A)-Binding Protein Are Distinct Processes Mediated by Two Epstein Barr Virus Proteins. PLOS ONE 2014, 9: e92593. PMID: 24705134, PMCID: PMC3976295, DOI: 10.1371/journal.pone.0092593.Peer-Reviewed Original ResearchConceptsHost gene expressionIntranuclear distributionZEBRA mutantsReplication proteinsNuclear translocationGene expressionEssential replication proteinViral replication proteinsDownstream viral genesViral replication compartmentsLytic replicationNew protein synthesisBZIP proteinsGlobal shutoffViral alkaline nucleaseReplication compartmentsPABPCEssential functionsEpstein-Barr virus proteinsHost shutoffViral genesLytic programProtein synthesisBinding proteinProtein
2012
Tracking expression and subcellular localization of RNA and protein species using high-throughput single cell imaging flow cytometry
Borah S, Nichols LA, Hassman LM, Kedes DH, Steitz JA. Tracking expression and subcellular localization of RNA and protein species using high-throughput single cell imaging flow cytometry. RNA 2012, 18: 1573-1579. PMID: 22745225, PMCID: PMC3404377, DOI: 10.1261/rna.033126.112.Peer-Reviewed Original ResearchConceptsKaposi's sarcoma-associated herpesvirusSarcoma-associated herpesvirusSubcellular localizationProtein moleculesHigh-throughput approachPAN RNAProtein speciesNoncoding RNAsNuclear RNAProtein C1Imaging Flow CytometryFlow cytometryRNANuclear translocationHigh-throughput applicationsLytic phaseViral RNATranslocationExpressionLocalizationCellsHeterogeneous populationPABPC1CytometryMoleculesEBV and human microRNAs co‐target oncogenic and apoptotic viral and human genes during latency
Riley KJ, Rabinowitz GS, Yario TA, Luna JM, Darnell RB, Steitz JA. EBV and human microRNAs co‐target oncogenic and apoptotic viral and human genes during latency. The EMBO Journal 2012, 31: 2207-2221. PMID: 22473208, PMCID: PMC3343464, DOI: 10.1038/emboj.2012.63.Peer-Reviewed Original ResearchConceptsHuman microRNAsLatent membrane protein 1Viral miRNA functionHigh-throughput sequencingHuman miRNA targetsMiRNA-binding sitesMiRNA functionEBV BHRF1Human genesMiRNA targetsMRNA targetsCellular miRNAsMembrane protein 1MiRNA clusterHuman miRNAsGene expressionCell cycleReporter assaysDistinct binding sitesViral mRNAsMiRNAsLytic genesLytic switchProtein 1EBV latent membrane protein 1
1979
Binding of mammalian ribosomes to ms2 phage rna reveals an overlapping gene encoding a lysis function
Atkins J, Steitz J, Anderson C, Model P. Binding of mammalian ribosomes to ms2 phage rna reveals an overlapping gene encoding a lysis function. Cell 1979, 18: 247-256. PMID: 498271, DOI: 10.1016/0092-8674(79)90044-8.Peer-Reviewed Original ResearchConceptsMammalian ribosomesLysis functionE. coli cell-free systemAmino acid polypeptideCoat protein geneAmino acid sequence analysisPartial amino acid sequence analysisMS2 phage RNAAcid sequence analysisCell-free systemLysis genesNonsense mutantsSynthetase geneUAA codonProtein geneAcid polypeptideSite mutantsTranslation productsInitiator regionSecond codonCistronNonpermissive cellsSame proteinPhage RNAAUG triplet
1977
Differential requirements for polypeptide chain initiation complex formation at the three bacteriophage R17 initiator regions
Steitz J, Wahba A, Laughrea M, Moore P. Differential requirements for polypeptide chain initiation complex formation at the three bacteriophage R17 initiator regions. Nucleic Acids Research 1977, 4: 1-16. PMID: 325516, PMCID: PMC342405, DOI: 10.1093/nar/4.1.1.Peer-Reviewed Original Research
1975
F factor-mediated inhibition of bacteriophage T7 growth: Analysis of T7 RNA and protein synthesis In vivo and In vitro using male and female Escherichia coli
Condit RC, Steitz JA. F factor-mediated inhibition of bacteriophage T7 growth: Analysis of T7 RNA and protein synthesis In vivo and In vitro using male and female Escherichia coli. Journal Of Molecular Biology 1975, 98: 31-43. PMID: 1104867, DOI: 10.1016/s0022-2836(75)80099-4.Peer-Reviewed Original ResearchConceptsT7 growthProtein synthesisE. coliPolyacrylamide gel electrophoresisEscherichia coliPhage protein synthesisGel electrophoresisTranslation apparatusT7 proteinsPhage proteinsT7 infectionT7 DNAT7 RNAFaithful synthesisRNA synthesisProteinMale cellsRNAColiTranscriptionSimultaneous inhibitionSpecific modificationsT7InhibitionElectrophoresis
1974
Cistron specificity of 30S ribosomes heterologously reconstituted with components from Escherichia coli and Bacillus stearothermophilus.
Goldberg M, Steitz J. Cistron specificity of 30S ribosomes heterologously reconstituted with components from Escherichia coli and Bacillus stearothermophilus. Biochemistry 1974, 13: 2123-9. PMID: 4597073, DOI: 10.1021/bi00707a020.Peer-Reviewed Original ResearchDirect physical evidence for secondary structure in an isolated fragment of R17 bacteriophage mRNA
Gralla J, Steitz J, Crothers D. Direct physical evidence for secondary structure in an isolated fragment of R17 bacteriophage mRNA. Nature 1974, 248: 204-208. PMID: 4819414, DOI: 10.1038/248204a0.Peer-Reviewed Original ResearchSpecific recognition of the isolated R17 replicase initiator region by R17 coat protein
STEITZ J. Specific recognition of the isolated R17 replicase initiator region by R17 coat protein. Nature 1974, 248: 223-225. PMID: 4819415, DOI: 10.1038/248223a0.Peer-Reviewed Original Research
1973
Discriminatory Ribosome Rebinding of Isolated Regions of Protein Synthesis Initiation from the Ribonucleic Acid of Bacteriophage R17
Steitz J. Discriminatory Ribosome Rebinding of Isolated Regions of Protein Synthesis Initiation from the Ribonucleic Acid of Bacteriophage R17. Proceedings Of The National Academy Of Sciences Of The United States Of America 1973, 70: 2605-2609. PMID: 4582190, PMCID: PMC427065, DOI: 10.1073/pnas.70.9.2605.Peer-Reviewed Original ResearchConceptsR17 RNARibosome-binding siteProtein synthesis initiationEscherichia coli ribosomesPolypeptide chain initiationCoat protein regionRibosome bindingBacterial ribosomeRNA moleculesInitiator regionRibosome protectionSynthesis initiationMRNA moleculesInitiator codonColi ribosomesRibosomesNative RNABacteriophage R17Bacillus stearothermophilusRNAMessenger RNARibonucleic acidR17Replicase regionFragmentsSpecific recognition of non-initiator regions in RNA bacteriophage messengers by ribosomes of Bacillus stearothermophilus
Steitz J. Specific recognition of non-initiator regions in RNA bacteriophage messengers by ribosomes of Bacillus stearothermophilus. Journal Of Molecular Biology 1973, 73: 1-16. PMID: 4570382, DOI: 10.1016/0022-2836(73)90155-1.Peer-Reviewed Original ResearchBacillusBase SequenceBinding SitesCentrifugation, Density GradientChromatography, Thin LayerColiphagesDipeptidesEscherichia coliGenetic CodeNucleotidesPeptide Chain Initiation, TranslationalPeptide Initiation FactorsRibonucleasesRibosomesRNA, MessengerRNA, TransferRNA, ViralSpecies SpecificityTemperatureViral Proteins
1972
Oligonucleotide Sequence of Replicase Initiation Site in Qβ RNA
STEITZ J. Oligonucleotide Sequence of Replicase Initiation Site in Qβ RNA. Nature 1972, 236: 71-75. PMID: 4502455, DOI: 10.1038/newbio236071a0.Peer-Reviewed Original ResearchConceptsReplicase geneQβ RNAMajor coat proteinN-terminal sequenceCoat cistronTermination signalReplicase cistronNucleotide sequenceCoat proteinRNA genomeInitiator codonInitiation siteQβ replicaseGenesProteinBacteriophage QβCistronUGA suppressorRNAVirus particlesSequenceOligonucleotide sequencesProtein7GenomeReplicase
1970
Control of Translation by T4 Phage : Altered Ribosome Binding at R17 Initiation Sites
STEITZ J, DUBE S, RUDLAND P. Control of Translation by T4 Phage : Altered Ribosome Binding at R17 Initiation Sites. Nature 1970, 226: 824-827. PMID: 5444624, DOI: 10.1038/226824a0.Peer-Reviewed Original Research
1969
Polypeptide Chain Initiation: Nucleotide Sequences of the Three Ribosomal Binding Sites in Bacteriophage R17 RNA
STEITZ J. Polypeptide Chain Initiation: Nucleotide Sequences of the Three Ribosomal Binding Sites in Bacteriophage R17 RNA. Nature 1969, 224: 957-964. PMID: 5360547, DOI: 10.1038/224957a0.Peer-Reviewed Original Research
1968
Identification of the A protein as a structural component of bacteriophage R17
Steitz J. Identification of the A protein as a structural component of bacteriophage R17. Journal Of Molecular Biology 1968, 33: 923-936. PMID: 4178187, DOI: 10.1016/0022-2836(68)90328-8.Peer-Reviewed Original ResearchConceptsA proteinBacteriophage R17Amber mutantsMolecule of histidineProtein monomersProtein productsMajor polypeptidesMolecular weight estimatesStructural componentsPhage particlesR17Non-permissive hostsDefective particlesVirus particlesProteinGel filtrationHistidineCistronMutantsSpheroplastsPolypeptideHostCopiesIsolation of the A protein from bacteriophage R17
Steitz J. Isolation of the A protein from bacteriophage R17. Journal Of Molecular Biology 1968, 33: 937-945. PMID: 5700426, DOI: 10.1016/0022-2836(68)90329-x.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsBacteriophagesChromatographyDetergentsElectrophoresisHistidineMolecular WeightTritiumViral Proteins