2018
Caution needs to be taken when assigning transcription start sites to ends of protein-coding genes: a rebuttal
Sabath N, Vilborg A, Steitz JA, Shalgi R. Caution needs to be taken when assigning transcription start sites to ends of protein-coding genes: a rebuttal. Human Genomics 2018, 12: 32. PMID: 29945683, PMCID: PMC6020437, DOI: 10.1186/s40246-018-0164-4.Peer-Reviewed Original ResearchConceptsTranscription start siteTranscriptional readthroughStart siteOsmotic stressProtein-coding genesGenome-wide comparisonEnd of genesStress-mediated inductionMammalian stress responseNIH3T3 mouse cellsDe novo initiationTranscription initiationGene endMammalian cellsLong transcriptsNIH3T3 cellsMouse cellsSimilar transcriptsStress responseTSS-seqHuman cellsReadthroughNovo initiationDramatic inductionStress conditions
2016
Intronless β-Globin Reporter: A Tool for Studying Nuclear RNA Stability Elements
Brown JA, Steitz JA. Intronless β-Globin Reporter: A Tool for Studying Nuclear RNA Stability Elements. Methods In Molecular Biology 2016, 1428: 77-92. PMID: 27236793, PMCID: PMC5547891, DOI: 10.1007/978-1-4939-3625-0_5.Peer-Reviewed Original Research
2015
A heterotrimer model of the complete Microprocessor complex revealed by single-molecule subunit counting
Herbert KM, Sarkar SK, Mills M, De la Herran H, Neuman KC, Steitz JA. A heterotrimer model of the complete Microprocessor complex revealed by single-molecule subunit counting. RNA 2015, 22: 175-183. PMID: 26683315, PMCID: PMC4712668, DOI: 10.1261/rna.054684.115.Peer-Reviewed Original ResearchConceptsPri-miRNA substratesMicroprocessor complexHeterotrimeric complexDeletion constructsSingle-molecule subunit countingRNA-binding proteinFull-length proteinAbsence of RNAStem-loop structureSingle-molecule photobleachingSize exclusion chromatographyPresence of RNARNaseIII enzymesPhotobleaching assaysMicroRNA biogenesisSubunit countingMammalian cellsDroshaDGCR8Fluorescent proteinHuman cellsMultiple copiesRNAProteinExact stoichiometry
2013
Phosphorylation of DGCR8 Increases Its Intracellular Stability and Induces a Progrowth miRNA Profile
Herbert KM, Pimienta G, DeGregorio SJ, Alexandrov A, Steitz JA. Phosphorylation of DGCR8 Increases Its Intracellular Stability and Induces a Progrowth miRNA Profile. Cell Reports 2013, 5: 1070-1081. PMID: 24239349, PMCID: PMC3892995, DOI: 10.1016/j.celrep.2013.10.017.Peer-Reviewed Original ResearchConceptsMicroprocessor complexRNA-binding proteinRNase III enzymeInhibition of phosphatasesStem-loop structureERK/MAPKSpecific processing activityMiRNA expression profilesExtracellular cuesMiRNA biogenesisDrosha proteinPhosphorylation sitesPrimary miRNAMammalian cellsProtein stabilityExpression profilesDGCR8Intracellular stabilityHeLa cellsCellular levelMiRNA profilesPhosphorylationMRNA levelsProteinCells
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
2009
Subnuclear 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
2006
Identification of a Rapid Mammalian Deadenylation-Dependent Decay Pathway and Its Inhibition by a Viral RNA Element
Conrad NK, Mili S, Marshall EL, Shu MD, Steitz JA. Identification of a Rapid Mammalian Deadenylation-Dependent Decay Pathway and Its Inhibition by a Viral RNA Element. Molecular Cell 2006, 24: 943-953. PMID: 17189195, DOI: 10.1016/j.molcel.2006.10.029.Peer-Reviewed Original ResearchConceptsQuality control pathwaysViral RNA elementsPAN RNAPolyadenylated transcriptsMammalian cellsNuclear RNASuch transcriptsRNA elementsCellular RNAGene expressionNuclear accumulationNuclear extractsNaked RNARNADecay pathwaysTranscriptsDeadenylationDependent fashionPathwayDeadenylaseIntronsAccumulationMRNAHybridizationIntramolecular hybridizationThe Challenge of Viral snRNPs
CONRAD NK, FOK V, CAZALLA D, BORAH S, STEITZ JA. The Challenge of Viral snRNPs. Cold Spring Harbor Symposia On Quantitative Biology 2006, 71: 377-384. PMID: 17381320, DOI: 10.1101/sqb.2006.71.057.Peer-Reviewed Original ResearchConceptsNuclear noncoding RNAsHSURs 1Sarcoma-associated herpesvirusRibosomal protein L22Aggressive T-cell leukemiaT cell signalingViral gene expressionKaposi's sarcoma-associated herpesvirusHeterokaryon assayU RNADependent RNA degradationMammalian cellsNoncoding RNAsProtein L22Nuclear surveillanceRNA degradationHost mRNAsHost proteinsGene expressionMRNA transcriptsMutant virusHerpesvirus saimiriRNAImportant functionsRNAs
2003
Splicing-Dependent and -Independent Modes of Assembly for Intron-Encoded Box C/D snoRNPs in Mammalian Cells
Hirose T, Shu MD, Steitz JA. Splicing-Dependent and -Independent Modes of Assembly for Intron-Encoded Box C/D snoRNPs in Mammalian Cells. Molecular Cell 2003, 12: 113-123. PMID: 12887897, DOI: 10.1016/s1097-2765(03)00267-3.Peer-Reviewed Original ResearchConceptsBox C/D snoRNAsSplice siteSnoRNP proteinsD snoRNAsSnoRNP assemblyMammalian cellsHost intronBox C/D snoRNPsSmall nucleolar RNAsD snoRNPsRRNA modificationNucleolar RNAsHost genesActive splicingNts upstreamIntronsEfficient expressionSnoRNAsStable stemSplicingVivo analysisProteinAssemblyBlockage experimentsStem
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 componentComplexesCodonSubunitsMachineryHuR and mRNA stability
Brennan CM, Steitz* J. HuR and mRNA stability. Cellular And Molecular Life Sciences 2001, 58: 266-277. PMID: 11289308, PMCID: PMC11146503, DOI: 10.1007/pl00000854.Peer-Reviewed Original ResearchConceptsAU-rich elementsMessenger RNAsGene regulationMRNA decayPosttranscriptional gene regulationMRNA degradation pathwayDrosophila ELAVMammalian cellsHu familyHuR functionMRNA stabilityUntranslated regionStressed cellsProtein ligandsRole of HuRCultured cellsEnvironmental changesHuRDegradation pathwayRapid degradationImportant mechanismRegulationCellsELAVRNAs
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
1993
A base-pairing interaction between U2 and U6 small nuclear RNAs occurs in > 150S complexes in HeLa cell extracts: implications for the spliceosome assembly pathway.
Wassarman DA, Steitz JA. A base-pairing interaction between U2 and U6 small nuclear RNAs occurs in > 150S complexes in HeLa cell extracts: implications for the spliceosome assembly pathway. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 7139-7143. PMID: 8346227, PMCID: PMC47091, DOI: 10.1073/pnas.90.15.7139.Peer-Reviewed Original ResearchConceptsU6 small nuclear RNASmall nuclear RNAS100 extractsNuclear RNASer/Arg-rich (SR) proteinsBase pairingNuclear extractsLarge complexesArg-rich proteinsPre-RNA splicingSpliceosome assembly pathwayHeLa cell extractsHeLa nuclear extractsBase-pairing interactionsBase pair formsPossible functional relationshipRibonucleoprotein complexesSpliceosome complexMammalian cellsAssembly pathwaySplicing substratePsoralen crosslinkingGlycerol gradientsCell extractsSplicing
1988
Additional low-abundance human small nuclear ribonucleoproteins: U11, U12, etc.
Montzka KA, Steitz JA. Additional low-abundance human small nuclear ribonucleoproteins: U11, U12, etc. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 8885-8889. PMID: 2973606, PMCID: PMC282611, DOI: 10.1073/pnas.85.23.8885.Peer-Reviewed Original ResearchConceptsSmall nuclear ribonucleoproteinU12 small nuclear ribonucleoproteinsSm small nuclear ribonucleoproteinsTrimethylguanosine cap structureTwo-dimensional gel fractionationLow-abundance RNAsLower eukaryotesSmall RNAsMRNA processingMammalian cellsMRNA splicingNuclear ribonucleoproteinAdditional speciesCap structureNuclease sensitivityNew RNASm classSm epitopesRNAU11Gel fractionationPotential roleU12EukaryotesSplicingA 5S rRNA/L5 complex is a precursor to ribosome assembly in mammalian cells.
Steitz JA, Berg C, Hendrick JP, La Branche-Chabot H, Metspalu A, Rinke J, Yario T. A 5S rRNA/L5 complex is a precursor to ribosome assembly in mammalian cells. Journal Of Cell Biology 1988, 106: 545-556. PMID: 3279045, PMCID: PMC2115095, DOI: 10.1083/jcb.106.3.545.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutoantibodiesCell NucleolusCentrifugation, Density GradientElectrophoresis, Polyacrylamide GelFluorescent Antibody TechniqueFriend murine leukemia virusHeLa CellsHumansImmunoassayLeukemia, Erythroblastic, AcuteRibonucleoproteinsRibosomal ProteinsRibosomesRNA PrecursorsRNA, RibosomalRNA, Ribosomal, 5STumor Cells, CulturedConceptsRNA-protein complexesVivo pulse-chase experimentsRibosomal protein L5Pulse-chase experimentsProtein complexesProtein L5Mammalian cellsRNA moleculesMouse cellsLater stepsHeLa cellsProtein moietyRNPRibosomesNucleoliCellsComplexesAssemblyBiogenesisRRNAIndirect immunofluorescenceSubunitsRNAImmunofluorescence
1985
Transfer RNA is an essential component of the ubiquitin- and ATP-dependent proteolytic system.
Ciechanover A, Wolin SL, Steitz JA, Lodish HF. Transfer RNA is an essential component of the ubiquitin- and ATP-dependent proteolytic system. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 1341-1345. PMID: 2983338, PMCID: PMC397256, DOI: 10.1073/pnas.82.5.1341.Peer-Reviewed Original ResearchConceptsATP-dependent proteolytic systemProteolytic systemATP-dependent degradationATP-requiring reactionATP-dependent pathwayProteolytic activityProgression of cellsProtein substratesTransfer RNAGene activationMammalian cellsUncharged tRNAReticulocyte extractsProtein degradationTRNA fractionReticulocyte systemMouse cellsCell cycleUbiquitinEssential componentRNAGel electrophoresisTRNAConjugated proteinsAutoimmune sera
1984
The structure of mammalian small nuclear ribonucleoproteins. Identification of multiple protein components reactive with anti-(U1)ribonucleoprotein and anti-Sm autoantibodies.
Pettersson I, Hinterberger M, Mimori T, Gottlieb E, Steitz JA. The structure of mammalian small nuclear ribonucleoproteins. Identification of multiple protein components reactive with anti-(U1)ribonucleoprotein and anti-Sm autoantibodies. Journal Of Biological Chemistry 1984, 259: 5907-5914. PMID: 6232278, DOI: 10.1016/s0021-9258(18)91101-4.Peer-Reviewed Original ResearchConceptsSm small nuclear ribonucleoproteinsSmall nuclear ribonucleoproteinNuclear ribonucleoproteinProtein componentsAnti-Sm patient seraMultiple protein componentsSnRNP proteinsU6 RNAMammalian cellsDistinct polypeptidesAnti-Sm monoclonal antibodyRNA immunoprecipitationAnti-Sm autoantibodiesSnRNP polypeptidesProtein compositionSnRNP particlesProtein BMonoclonal antibodiesRibonucleoproteinIntriguing questionPolypeptideProteinBlot resultsMouse monoclonal antibodyEntire collectionU4 and U6 RNAs coexist in a single small nuclear ribonucleoprotein particle
Hashimoto C, Steitz J. U4 and U6 RNAs coexist in a single small nuclear ribonucleoprotein particle. Nucleic Acids Research 1984, 12: 3283-3293. PMID: 6201826, PMCID: PMC318745, DOI: 10.1093/nar/12.7.3283.Peer-Reviewed Original ResearchConceptsSmall nuclear ribonucleoproteinU6 RNARNA complexIntact small nuclear ribonucleoproteinRNA/RNA complexesHuman small nuclear ribonucleoproteinsSmall nuclear ribonucleoprotein particleRNA-RNA interactionsNuclear ribonucleoprotein particleSequence complementarityMammalian cellsNuclear ribonucleoproteinRibonucleoprotein particleSnRNP particlesRNABiological implicationsPolyacrylamide gelsProteinase KU4ComplexesSodium dodecyl sulfateRibonucleoproteinDodecyl sulfateU5U1
1983
Genes for two small cytoplasmic Ro RNAs are adjacent and appear to be single-copy in the human genome
Wolin S, Steitz J. Genes for two small cytoplasmic Ro RNAs are adjacent and appear to be single-copy in the human genome. Cell 1983, 32: 735-744. PMID: 6187471, DOI: 10.1016/0092-8674(83)90059-4.Peer-Reviewed Original ResearchConceptsHuman genomeRo RNAsSecondary structure homologyRNA polymerase IIISmall cytoplasmic ribonucleoproteinsClass III genesGenomic clonesMammalian cellsPolymerase IIIRNA componentStructure homologySingle copyCytoplasmic ribonucleoproteinHY5 RNAMouse cellsHuman cellsHY1Cell extractsGenesRNAGenomeRNAsHY3CellsMY1Structure and Function of Small Ribonucleoproteins from Eukaryotic Cells
Steitz JA, Berg C, Gottlieb E, Hardin JA, Hashimoto C, Hendrick JP, Hinterberger M, Krikeles M, Lerner MR, Mount SM, Pettersson I, Rinke J, Rosa M, Wolin S. Structure and Function of Small Ribonucleoproteins from Eukaryotic Cells. 1983, 12: 309-317. PMID: 7166547, DOI: 10.1016/b978-0-12-501650-6.50023-7.Peer-Reviewed Original ResearchConceptsSmall ribonucleoproteinLa proteinRNA polymerase III transcription factorSmall RNA-protein complexesDrosophila U1 RNAU1 small nuclearRNA-protein complexesHnRNA splicingEukaryotic cellsSmall cytoplasmicMammalian cellsRRNA precursorTranscription factorsSmall nuclearU1 RNASplice junctionsRibonucleoproteinLa ribonucleoproteinsFurther characterizationProteinRelated diseasesCellsSplicingTRNARNA