2014
The Noncoding RNA Revolution—Trashing Old Rules to Forge New Ones
Cech TR, Steitz JA. The Noncoding RNA Revolution—Trashing Old Rules to Forge New Ones. Cell 2014, 157: 77-94. PMID: 24679528, DOI: 10.1016/j.cell.2014.03.008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsChromatinGene Expression RegulationGenomeHumansRibonucleoproteinsRNA, CatalyticRNA, Long NoncodingRNA, UntranslatedConceptsBiological functionsRNA-protein complexesLevel of transcriptionForeign nucleic acidsMost ncRNAsLong ncRNAsNcRNA researchRNA processingGenome rearrangementsNucleic acidsNoncoding RNAsGene expressionRNA structureNcRNAsBase pairingDNA synthesisRemarkable varietySnoRNPsRiboswitchGenomeSnRNPsRNAsRibosomesTranscriptionTelomerase
2011
Posttranscriptional activation of gene expression in Xenopus laevis oocytes by microRNA–protein complexes (microRNPs)
Mortensen RD, Serra M, Steitz JA, Vasudevan S. Posttranscriptional activation of gene expression in Xenopus laevis oocytes by microRNA–protein complexes (microRNPs). Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 8281-8286. PMID: 21536868, PMCID: PMC3100953, DOI: 10.1073/pnas.1105401108.Peer-Reviewed Original ResearchConceptsMicroRNA–protein complexesProtein kinase AIIXenopus laevis oocytesImmature Xenopus laevis oocytesGene expression activationMammalian cell linesLaevis oocytesHuman Ago2Target reporterMammalian cellsExpression activationMyt1 kinaseGene expressionPosttranscriptional activationRegulated expressionSpecific mRNAsPhysiological relevanceQuiescent cellsMicroRNAsOocyte stateCell linesOocytesReporterCAMP levelsExpression
2010
Noncoding RNPs of Viral Origin
Steitz J, Borah S, Cazalla D, Fok V, Lytle R, Mitton-Fry R, Riley K, Samji T. Noncoding RNPs of Viral Origin. Cold Spring Harbor Perspectives In Biology 2010, 3: a005165. PMID: 20719877, PMCID: PMC3039937, DOI: 10.1101/cshperspect.a005165.Peer-Reviewed Original Research
2009
miRNPs: versatile regulators of gene expression in vertebrate cells1
Steitz JA, Vasudevan S. miRNPs: versatile regulators of gene expression in vertebrate cells1. Biochemical Society Transactions 2009, 37: 931-935. PMID: 19754429, DOI: 10.1042/bst0370931.Peer-Reviewed Original ResearchConceptsPost-transcriptional controlAssociation of Ago2Role of miRNAsImmature Xenopus oocytesTNFalpha AREProtein FXR1Contact-inhibited cellsTranslational regulationTranslation activationVersatile regulatorsTranslational efficiencyNegative regulatorGene expressionSpecific miRNACell cycleEffector moleculesCell growthXenopus oocytesAgo2FXR1A Conserved WD40 Protein Binds the Cajal Body Localization Signal of scaRNP Particles
Tycowski KT, Shu MD, Kukoyi A, Steitz JA. A Conserved WD40 Protein Binds the Cajal Body Localization Signal of scaRNP Particles. Molecular Cell 2009, 34: 47-57. PMID: 19285445, PMCID: PMC2700737, DOI: 10.1016/j.molcel.2009.02.020.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAnimalsBase SequenceCell LineChromatography, AffinityCoiled BodiesDrosophila melanogasterDrosophila ProteinsHeLa CellsHumansMolecular Sequence DataNucleic Acid ConformationRecombinant Fusion ProteinsRegulatory Sequences, Ribonucleic AcidRibonucleoproteinsRNA-Binding ProteinsSequence AlignmentConceptsCAB boxCB localizationSmall Cajal bodyWD40 proteinsRNP functionCajal bodiesLocalization signalACA motifDomain RNATelomerase RNAHuman homologPosttranscriptional modificationsSmall nuclearWDR79ScaRNAsRNA elementsCentral playerUV crosslinkNuclear RNPCore proteinRNAProteinAdditional interactionsBindingLocalizationSubnuclear compartmentalization of transiently expressed polyadenylated pri-microRNAs: Processing at transcription sites or accumulation in SC35 foci
Pawlicki JM, Steitz JA. Subnuclear compartmentalization of transiently expressed polyadenylated pri-microRNAs: Processing at transcription sites or accumulation in SC35 foci. Cell Cycle 2009, 8: 345-356. PMID: 19177009, PMCID: PMC3004524, DOI: 10.4161/cc.8.3.7494.Peer-Reviewed Original ResearchConceptsPri-miRNA processingPri-miRNAsTranscription sitesPrimary miRNA transcriptsPri-miRNA transcriptsPre-miRNA hairpinsRNA polymerase IIASF/SF2Splicing factor SC35Target messenger RNAsNumber of proteinsMiRNA biogenesisMiRNA transcriptsNuclear organizationMRNA metabolismPolymerase IINuclear fociProlyl isomeraseFactor SC35Subnuclear compartmentalizationPri-microRNAsMammalian cellsSC35 domainsGene expressionSC35
2008
Primary microRNA transcript retention at sites of transcription leads to enhanced microRNA production
Pawlicki JM, Steitz JA. Primary microRNA transcript retention at sites of transcription leads to enhanced microRNA production. Journal Of Cell Biology 2008, 182: 61-76. PMID: 18625843, PMCID: PMC2447899, DOI: 10.1083/jcb.200803111.Peer-Reviewed Original ResearchMeSH KeywordsChromatinExonsHeLa CellsHumansIntronsMicroRNAsMRNA Cleavage and Polyadenylation FactorsNuclear ProteinsPolyadenylationRegulatory Sequences, Nucleic AcidRibonucleoproteinsRNA Polymerase IIIRNA Processing, Post-TranscriptionalRNA TransportRNA, MessengerRNA, ViralSequence DeletionSerine-Arginine Splicing FactorsSubcellular FractionsTranscription, GeneticConceptsPri-miRNAsTranscription sitesEndogenous pri-miRNAsPrimary miRNA transcriptsPri-miRNA processingSplicing factor SC35Viral RNA elementsHigh nuclear levelsMiRNA biogenesisMiRNA transcriptionMiRNA transcriptsNuclear stepsPrecursor miRNAsNuclear fociFactor SC35MicroRNA productionRNA elementsGene expressionTranscription leadNuclear fractionNuclear levelsTranscriptionMiRNAsProcessing signalsBiogenesis
2007
Switching from Repression to Activation: MicroRNAs Can Up-Regulate Translation
Vasudevan S, Tong Y, Steitz JA. Switching from Repression to Activation: MicroRNAs Can Up-Regulate Translation. Science 2007, 318: 1931-1934. PMID: 18048652, DOI: 10.1126/science.1149460.Peer-Reviewed Original ResearchMeSH Keywords3' Untranslated RegionsArgonaute ProteinsBase PairingCell CycleCell LineCell ProliferationComputational BiologyEukaryotic Initiation Factor-2Gene Expression RegulationHeLa CellsHMGA2 ProteinHumansInterphaseMicroRNAsProtein BiosynthesisRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerTransfectionTumor Necrosis Factor-alphaUp-RegulationConceptsAU-rich elementsCell cycle arrestCycle arrestUntranslated regionMental retardation-related protein 1MicroRNA target sitesMicroRNA let-7Messenger RNA (mRNA) 3' untranslated regionsRegulates TranslationTranslation regulationTarget mRNAsGene expressionCell cycleCommon functionProtein 1ArgonauteTarget siteActivation signalsRepressionTumor necrosis factor-alpha mRNAMRNARegulationActivationArrestMicroRNPsTarget mRNAs are repressed as efficiently by microRNA-binding sites in the 5′ UTR as in the 3′ UTR
Lytle JR, Yario TA, Steitz JA. Target mRNAs are repressed as efficiently by microRNA-binding sites in the 5′ UTR as in the 3′ UTR. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 9667-9672. PMID: 17535905, PMCID: PMC1887587, DOI: 10.1073/pnas.0703820104.Peer-Reviewed Original ResearchConceptsInternal ribosome entry siteTarget mRNAsMiRNA-mediated repressionRepression of translationLuciferase reporter mRNAMiRNA target sitesInitiation of translationMiRNA-binding sitesHuman HeLa cellsRibosome entry siteMicroRNA-binding sitesLet-7 complementary sitesHuman Ago2Reporter mRNAMicroRNAs (miRNAs) bindEndogenous mRNATranslational efficiencyLet-7a miRNAUTRProtein synthesisDNA transfectionComplementary sitesHeLa cellsEntry siteTarget siteAU-Rich-Element-Mediated Upregulation of Translation by FXR1 and Argonaute 2
Vasudevan S, Steitz JA. AU-Rich-Element-Mediated Upregulation of Translation by FXR1 and Argonaute 2. Cell 2007, 128: 1105-1118. PMID: 17382880, PMCID: PMC3430382, DOI: 10.1016/j.cell.2007.01.038.Peer-Reviewed Original ResearchMeSH Keywords3' Untranslated RegionsArgonaute ProteinsCell CycleCell LineChromatography, AffinityCulture Media, Serum-FreeEukaryotic Initiation Factor-2Genes, ReporterHumansLuciferases, FireflyMonocytesPeptide Initiation FactorsPolyribosomesProtein BiosynthesisRegulatory Sequences, Ribonucleic AcidRibonucleoproteinsRNA-Binding ProteinsSerumTumor Necrosis Factor-alphaUp-RegulationConceptsAU-rich elementsArgonaute 2Posttranscriptional regulatory systemsAffinity purification methodShRNA knockdown experimentsCell cycle arrestHuman cell linesTranslation activationRegulatory signalsMRNA stabilityGene expressionSerum starvationAU-RichFXR1Activation roleRegulatory systemProtein 1Cell linesMRNA levelsNew insightsDevelopmental consequencesTranslation conditionsUpregulationDirect evidencePurification method
2006
Epstein-Barr virus noncoding RNAs are confined to the nucleus, whereas their partner, the human La protein, undergoes nucleocytoplasmic shuttling
Fok V, Friend K, Steitz JA. Epstein-Barr virus noncoding RNAs are confined to the nucleus, whereas their partner, the human La protein, undergoes nucleocytoplasmic shuttling. Journal Of Cell Biology 2006, 173: 319-325. PMID: 16682524, PMCID: PMC2063832, DOI: 10.1083/jcb.200601026.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAnimalsAntibiotics, AntineoplasticAutoantigensCell LineCell Line, TumorCell NucleusDactinomycinFatty Acids, UnsaturatedFemaleHeLa CellsHerpesvirus 4, HumanHumansKaryopherinsMiceNIH 3T3 CellsOocytesProtein BindingRibonucleoproteinsRNA TransportRNA, UntranslatedRNA, ViralXenopus laevis
2004
A molecular link between SR protein dephosphorylation and mRNA export
Huang Y, Yario TA, Steitz JA. A molecular link between SR protein dephosphorylation and mRNA export. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 9666-9670. PMID: 15210956, PMCID: PMC470732, DOI: 10.1073/pnas.0403533101.Peer-Reviewed Original ResearchConceptsNuclear export factor 1Multiple RNA-binding proteinsMRNA-protein complexesSR protein dephosphorylationMRNA nuclear exportASF/SF2RNA-binding proteinMRNA exportProtein dephosphorylationProtein complexesProtein adaptersNuclear exportSpliced mRNAPhosphorylation stateMolecular linkFactor 1MRNAHigh affinityMetazoansDephosphorylationExportComplexesSerineAdapterProtein
2001
Communication of the Position of Exon-Exon Junctions to the mRNA Surveillance Machinery by the Protein RNPS1
Lykke-Andersen J, Shu M, Steitz J. Communication of the Position of Exon-Exon Junctions to the mRNA Surveillance Machinery by the Protein RNPS1. Science 2001, 293: 1836-1839. PMID: 11546874, DOI: 10.1126/science.1062786.Peer-Reviewed Original ResearchMeSH Keywords3' Untranslated RegionsAnimalsCell LineDNA-Binding ProteinsExonsFungal ProteinsGlobinsHeLa CellsHumansMacromolecular SubstancesMiceModels, BiologicalPrecipitin TestsProtein BindingRecombinant Fusion ProteinsRibonucleoproteinsRNA HelicasesRNA SplicingRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsTrans-ActivatorsTransfectionConceptsNonsense-mediated decayExon-exon junctionsMRNA surveillanceMRNA quality controlMRNA surveillance machinerySelective nuclear exportBeta-globin mRNAPremature termination codonUpf complexMature mRNASurveillance machineryNuclear exportAberrant mRNAsMammalian cellsTermination codonUntranslated regionSplice junctionsRNPS1MRNADual roleCentral componentComplexesCodonSubunitsMachinery
1999
Initial recognition of U12-dependent introns requires both U11/5′ splice-site and U12/branchpoint interactions
Frilander M, Steitz J. Initial recognition of U12-dependent introns requires both U11/5′ splice-site and U12/branchpoint interactions. Genes & Development 1999, 13: 851-863. PMID: 10197985, PMCID: PMC316595, DOI: 10.1101/gad.13.7.851.Peer-Reviewed Original ResearchAdenoviridaeBlotting, NorthernDose-Response Relationship, DrugEvolution, MolecularFicusinHeLa CellsHeterogeneous-Nuclear RibonucleoproteinsHumansIntronsModels, GeneticOligonucleotidesRibonuclease HRibonucleoprotein, U4-U6 Small NuclearRibonucleoproteinsRibonucleoproteins, Small NuclearRNA SplicingTime Factors
1998
HNS, a nuclear-cytoplasmic shuttling sequence in HuR
Fan X, Steitz J. HNS, a nuclear-cytoplasmic shuttling sequence in HuR. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 15293-15298. PMID: 9860962, PMCID: PMC28036, DOI: 10.1073/pnas.95.26.15293.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsAntigens, SurfaceCell NucleusConserved SequenceCytoplasmELAV ProteinsELAV-Like Protein 1HeLa CellsHeterogeneous-Nuclear Ribonucleoprotein KHumansMiceMolecular Sequence DataRecombinant ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerSequence AlignmentSequence Homology, Amino AcidTransfectionXenopusConceptsHeterogeneous nuclear ribonucleoprotein KNuclear localization signal activityClassical nuclear localization signalAU-rich element-containing mRNAsExport of mRNAHeterogeneous nuclear ribonucleoprotein A1Nuclear export signalNuclear localization signalNuclear transport processRNA-binding proteinAU-rich elementsExport signalLocalization signalM9 sequenceNuclear poresDomain sequencesCytoplasmic compartmentUntranslated regionLabile mRNAsCell nucleiSpecific signalsHuRProteinBidirectional transportMRNAClassification of gas5 as a Multi-Small-Nucleolar-RNA (snoRNA) Host Gene and a Member of the 5′-Terminal Oligopyrimidine Gene Family Reveals Common Features of snoRNA Host Genes
Smith C, Steitz J. Classification of gas5 as a Multi-Small-Nucleolar-RNA (snoRNA) Host Gene and a Member of the 5′-Terminal Oligopyrimidine Gene Family Reveals Common Features of snoRNA Host Genes. Molecular And Cellular Biology 1998, 18: 6897-6909. PMID: 9819378, PMCID: PMC109273, DOI: 10.1128/mcb.18.12.6897.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsBase SequenceCell DivisionCell NucleolusCloning, MolecularHumansMembrane ProteinsMiceMolecular Sequence DataMultigene FamilyProtein BiosynthesisRibonucleoproteinsRibosomesRNA SplicingRNA, AntisenseRNA, MessengerRNA, Small NuclearRNA, Small NucleolarTranscription, GeneticConceptsHost genesGene familyGAS5 geneBox C/D snoRNAsSnoRNA host genesHost gene transcriptsCell growthInhibition of translationSmall nucleolar RNA host geneSmall nucleolarD snoRNAsGAS5 transcriptsMRNP particlesSpecific transcriptsGene transcriptsGenesTranscriptsSnoRNAsRNASequenceIntronsCommon featureRibosomesRRNAFamily
1995
Isolation and characterization of a novel, low abundance hnRNP protein: A0.
Myer VE, Steitz JA. Isolation and characterization of a novel, low abundance hnRNP protein: A0. RNA 1995, 1: 171-82. PMID: 7585247, PMCID: PMC1369071.Peer-Reviewed Original ResearchConceptsHnRNP A0HnRNP proteinsGlycine-rich C-terminusHeterogeneous nuclear ribonucleoprotein complexesB familyLow-abundance membersPre-messenger RNATwo-dimensional gel electrophoresisCharacteristic primary structureNuclear ribonucleoprotein complexesVariety of proteinsB family membersRibonucleoprotein complexesHnRNP complexesMammalian cellsMRNA stabilityC-terminusPrimary structureProtease mappingProteinRNA probesGel electrophoresisBasic proteinMajor classesRNA
1994
The Epstein-Barr virus (EBV) small RNA EBER1 binds and relocalizes ribosomal protein L22 in EBV-infected human B lymphocytes.
Toczyski DP, Matera AG, Ward DC, Steitz JA. The Epstein-Barr virus (EBV) small RNA EBER1 binds and relocalizes ribosomal protein L22 in EBV-infected human B lymphocytes. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 3463-3467. PMID: 8159770, PMCID: PMC43597, DOI: 10.1073/pnas.91.8.3463.Peer-Reviewed Original ResearchConceptsEpstein-Barr virusHuman B lymphocytesB lymphocytesEBV-positive lymphocytesEBV-positive cellsEBER1 RNAUninfected human cellsCertain patientsEBER1Ribosomal protein L22LymphocytesChromosomal translocationsOncogenic herpesvirusProtein L22Situ hybridizationUninfected cell extractsNucleoplasmic stainingVivoCell transformationHigh levelsHuman cellsCellsPatientsLeukemiaCellular proteins
1992
Splicing Takes a Holliday
Steitz J. Splicing Takes a Holliday. Science 1992, 257: 888-889. PMID: 1386941, DOI: 10.1126/science.1386941.Peer-Reviewed Original ResearchThe low-abundance U11 and U12 small nuclear ribonucleoproteins (snRNPs) interact to form a two-snRNP complex.
Wassarman KM, Steitz JA. The low-abundance U11 and U12 small nuclear ribonucleoproteins (snRNPs) interact to form a two-snRNP complex. Molecular And Cellular Biology 1992, 12: 1276-1285. PMID: 1372090, PMCID: PMC369560, DOI: 10.1128/mcb.12.3.1276.Peer-Reviewed Original Research