2017
Settling the m6A debate: methylation of mature mRNA is not dynamic but accelerates turnover
Rosa-Mercado NA, Withers JB, Steitz JA. Settling the m6A debate: methylation of mature mRNA is not dynamic but accelerates turnover. Genes & Development 2017, 31: 957-958. PMID: 28637691, PMCID: PMC5495124, DOI: 10.1101/gad.302695.117.Peer-Reviewed Original ResearchConceptsPre-mRNA splicing eventsPost-transcriptional modificationsMRNA biogenesisDifferent subcellular fractionsMRNA biologySplicing eventsMature mRNABiochemical approachesRNA transcriptsPivotal regulatorMethylation levelsHeLa cellsSubcellular fractionsRNA nucleosidesMethylationTranscriptsBiogenesisChromatinSplicingMethyladenosineExonsGenesRNABiologyRegulator
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
2007
Target 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 site
2004
Transportins 1 and 2 are redundant nuclear import factors for hnRNP A1 and HuR
Rebane A, Aab A, Steitz JA. Transportins 1 and 2 are redundant nuclear import factors for hnRNP A1 and HuR. RNA 2004, 10: 590-599. PMID: 15037768, PMCID: PMC1370549, DOI: 10.1261/rna.5224304.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAmino Acid SequenceAntigens, SurfaceBeta KaryopherinsCell NucleusELAV ProteinsELAV-Like Protein 1HeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHumansMolecular Sequence DataMutationProtein Structure, TertiaryRan GTP-Binding ProteinReceptors, Cytoplasmic and NuclearRNA-Binding ProteinsSequence Analysis, ProteinConceptsHnRNP A1Transportin-1Import factorsDigitonin-permeabilized HeLa cellsNuclear import factorsMRNA-binding proteinRecombinant hnRNP A1Binding of HuRImp betaImport pathwayCargo specificityNuclear importExport receptorTransportin-2TransportinTransport signalHeLa cellsLikely actsHuRTrn1ProteinInteraction studiesImportTRN2RanGTP
1996
More Sm snRNAs from Vertebrate Cells
Yu Y, Tarn W, Yario T, Steitz J. More Sm snRNAs from Vertebrate Cells. Experimental Cell Research 1996, 229: 276-281. PMID: 8986610, DOI: 10.1006/excr.1996.0372.Peer-Reviewed Original ResearchA Novel Spliceosome Containing U11, U12, and U5 snRNPs Excises a Minor Class (AT–AC) Intron In Vitro
Tarn W, Steitz J. A Novel Spliceosome Containing U11, U12, and U5 snRNPs Excises a Minor Class (AT–AC) Intron In Vitro. Cell 1996, 84: 801-811. PMID: 8625417, DOI: 10.1016/s0092-8674(00)81057-0.Peer-Reviewed Original ResearchMeSH KeywordsBase CompositionBase SequenceBlotting, NorthernCell NucleusHeLa CellsHumansMolecular Sequence DataNucleic Acid ConformationOligodeoxyribonucleotidesPlasmidsPolymerase Chain ReactionRibonuclease HRibonucleoprotein, U5 Small NuclearRibonucleoproteins, Small NuclearRNA PrecursorsRNA SplicingConceptsU5 small nuclear ribonucleoproteinSmall nuclear ribonucleoproteinU12 small nuclear ribonucleoproteinsMinor class intronsProtein coding genesPre-mRNA substrateNative gel electrophoresisCoding genesBranch site sequenceSplicing complexesNuclear ribonucleoproteinPre-mRNAP120 geneLariat intermediateSite sequenceIntronsHeLa cellsEssential roleSplicingGel electrophoresisBranch siteGenesU12Minor classU11
1993
Mutations in the conserved loop of human U5 snRNA generate use of novel cryptic 5′ splice sites in vivo.
Cortes JJ, Sontheimer EJ, Seiwert SD, Steitz JA. Mutations in the conserved loop of human U5 snRNA generate use of novel cryptic 5′ splice sites in vivo. The EMBO Journal 1993, 12: 5181-5189. PMID: 8262061, PMCID: PMC413781, DOI: 10.1002/j.1460-2075.1993.tb06213.x.Peer-Reviewed Original ResearchConceptsSplice siteRabbit beta-globin geneBeta-globin transcriptsBeta-globin geneU5 genesConserved loopMRNA splicingU5 snRNASecond intronFirst exonExon sequencesLoop mutantsSecond exonExpression vectorTransient transfectionCryptic sitesNovel siteHeLa cellsGT dinucleotideExonsExon 1U5 sequencesSnRNAMutationsVivo systemRare scleroderma autoantibodies to the U11 small nuclear ribonucleoprotein and to the trimethylguanosine cap of U small nuclear RNAs.
Gilliam AC, Steitz JA. Rare scleroderma autoantibodies to the U11 small nuclear ribonucleoprotein and to the trimethylguanosine cap of U small nuclear RNAs. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 6781-6785. PMID: 8341699, PMCID: PMC47016, DOI: 10.1073/pnas.90.14.6781.Peer-Reviewed Original ResearchConceptsSmall nuclear ribonucleoprotein particleTrimethylguanosine capLow-abundance membersSmall nuclear RNASmall nuclear ribonucleoproteinNuclear ribonucleoprotein particleGlycerol gradient fractionsU RNAU11 small nuclear ribonucleoproteinsSnRNP complexTargeted degradationNuclear RNANuclear ribonucleoproteinRibonucleoprotein particleNuclear extractsSm classProtein componentsHeLa cellsRNPGradient fractionsRNAProteinScleroderma seraRibonucleoproteinCosediments
1992
Three Novel Functional Variants of Human U5 Small Nuclear RNA
Sontheimer E, Steitz J. Three Novel Functional Variants of Human U5 Small Nuclear RNA. Molecular And Cellular Biology 1992, 12: 734-746. DOI: 10.1128/mcb.12.2.734-746.1992.Peer-Reviewed Original ResearchU5 small nuclear RNASmall nuclear RNANuclear RNAHeLa cellsSmall nuclear ribonucleoprotein particleTri-snRNP complexOligonucleotide-directed RNase H cleavageNuclear ribonucleoprotein particleNovel functional variantsFull-length speciesAffinity-purified spliceosomesTrimethylguanosine capAlternative splicingShorter speciesRibonucleoprotein particleMinimal domainHeLa extractsPrimer extensionFunctional variantsHigh abundanceBase changesNorthern blottingAbundant formUS variantsRNAThree Novel Functional Variants of Human U5 Small Nuclear RNA
Sontheimer E, Steitz J. Three Novel Functional Variants of Human U5 Small Nuclear RNA. Molecular And Cellular Biology 1992, 12: 734-746. DOI: 10.1128/mcb.12.2.734-746.1992.Peer-Reviewed Original ResearchU5 small nuclear RNASmall nuclear RNAHeLa cellsNuclear RNAAffinity-purified spliceosomesSmall nuclear ribonucleoproteinTri-snRNP complexFull-length speciesSaccharomyces cerevisiaeSplicing extractsPrimer extensionUS variantsHeLa extractsAlternative splicingRNA blotsShort speciesNuclear ribonucleoproteinBase changesMinimal domainHigher abundanceNorthern blottingRNAHeLaAbundant formSplicingThree novel functional variants of human U5 small nuclear RNA.
Sontheimer EJ, Steitz JA. Three novel functional variants of human U5 small nuclear RNA. Molecular And Cellular Biology 1992, 12: 734-746. PMID: 1310151, PMCID: PMC364287, DOI: 10.1128/mcb.12.2.734.Peer-Reviewed Original ResearchConceptsU5 small nuclear RNASmall nuclear RNANuclear RNAHeLa cellsSmall nuclear ribonucleoprotein particleTri-snRNP complexOligonucleotide-directed RNase H cleavageNuclear ribonucleoprotein particleNovel functional variantsFull-length speciesAffinity-purified spliceosomesTrimethylguanosine capAlternative splicingShorter speciesRibonucleoprotein particleMinimal domainHeLa extractsPrimer extensionFunctional variantsHigh abundanceBase changesNorthern blottingAbundant formRNASpecies
1991
Multiple processing-defective mutations in a mammalian histone pre-mRNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro.
Bond UM, Yario TA, Steitz JA. Multiple processing-defective mutations in a mammalian histone pre-mRNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro. Genes & Development 1991, 5: 1709-1722. PMID: 1885007, DOI: 10.1101/gad.5.9.1709.Peer-Reviewed Original ResearchConceptsHistone downstream elementHistone pre-mRNAMammalian histone pre-mRNAsPre-mRNAHeLa cellsBase pair regionMammalian histonesU7 geneSm snRNPsU7 snRNPGenetic evidenceU7 snRNAUnexpected toleranceU7 RNANuclear extractsDownstream elementsSuppressor geneCompensatory changesGenesBlock substitutionsRNAVivoSnRNPsSnRNPCells
1989
U3, U8 and U13 comprise a new class of mammalian snRNPs localized in the cell nucleolus.
Tyc K, Steitz JA. U3, U8 and U13 comprise a new class of mammalian snRNPs localized in the cell nucleolus. The EMBO Journal 1989, 8: 3113-3119. PMID: 2531075, PMCID: PMC401391, DOI: 10.1002/j.1460-2075.1989.tb08463.x.Peer-Reviewed Original Research
1988
A 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
1987
Accurate 5' splice-site selection in mouse kappa immunoglobulin light chain premessenger RNAs is not cell-type-specific.
Kedes DH, Steitz JA. Accurate 5' splice-site selection in mouse kappa immunoglobulin light chain premessenger RNAs is not cell-type-specific. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 7928-7932. PMID: 3120179, PMCID: PMC299449, DOI: 10.1073/pnas.84.22.7928.Peer-Reviewed Original ResearchConceptsSplice site selectionSplice siteHeLa cellsLight chain transcriptsChain transcriptsV-J recombinationMouse kappa light chainsSplicing machineryPremessenger RNAConstant exonsGene sequencesKappa-producing cellsSynthetic transcriptsGene expressionNuclear extractsMouse B lymphocytesUpstream sitesTranscriptsExonsSequenceLight chainCellsPotential mechanismsSitesGenesStructural Analysis of the Human U3 Ribonucleoprotein Particle Reveal a Conserved Sequence Available for Base Pairing with Pre-rRna
Parker K, Steitz J. Structural Analysis of the Human U3 Ribonucleoprotein Particle Reveal a Conserved Sequence Available for Base Pairing with Pre-rRna. Molecular And Cellular Biology 1987, 7: 2899-2913. DOI: 10.1128/mcb.7.8.2899-2913.1987.Peer-Reviewed Original ResearchProtein-RNA interactionsSecondary structureSubsequent reverse transcriptionRNA secondary structureHuman U3Phosphorylated proteinsConserved sequencesProcessing eventsPre-rRNAAlternative functionsBase pairsNucleotides -159Specific nucleasesHeLa cellsProtein constituentsRNase ABase pairingRNPProteinNonphosphorylated proteinsRRNAReverse transcriptionSequenceKilodaltonsNucleotides 65Structural analysis of the human U3 ribonucleoprotein particle reveal a conserved sequence available for base pairing with pre-rRNA.
Parker KA, Steitz JA. Structural analysis of the human U3 ribonucleoprotein particle reveal a conserved sequence available for base pairing with pre-rRNA. Molecular And Cellular Biology 1987, 7: 2899-2913. PMID: 2959855, PMCID: PMC367909, DOI: 10.1128/mcb.7.8.2899.Peer-Reviewed Original ResearchConceptsProtein-RNA interactionsSecondary structureSubsequent reverse transcriptionRNA secondary structureHuman U3Phosphorylated proteinsRibonucleoprotein particleProcessing eventsAlternative functionsBase pairsNucleotides -159Specific nucleasesHeLa cellsProtein constituentsRNase ARNPProteinNonphosphorylated proteinsRRNAReverse transcriptionSequenceKilodaltonsNucleotides 65Specific reagentsTranscription
1986
Characterization of the DNA-binding protein antigen Ku recognized by autoantibodies from patients with rheumatic disorders.
Mimori T, Hardin JA, Steitz JA. Characterization of the DNA-binding protein antigen Ku recognized by autoantibodies from patients with rheumatic disorders. Journal Of Biological Chemistry 1986, 261: 2274-2278. PMID: 3511059, DOI: 10.1016/s0021-9258(17)35929-x.Peer-Reviewed Original ResearchConceptsKu proteinNovel DNA-binding proteinAnti-Ku antibodiesDNA-binding proteinsHigh molecular weight nucleic acidsExtracts of cellsKu antigenDa subunitChromatinHeLa cellsScleroderma-polymyositis overlap syndromeBiochemical natureProteinWeight nucleic acidsLarge formNucleic acidsOverlap syndromeRheumatic disordersCertain patientsAntibodiesAntigenAutoantibodiesCellsImmunoaffinity column chromatographyPatients
1984
The Ro small cytoplasmic ribonucleoproteins: identification of the antigenic protein and its binding site on the Ro RNAs.
Wolin SL, Steitz JA. The Ro small cytoplasmic ribonucleoproteins: identification of the antigenic protein and its binding site on the Ro RNAs. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 1996-2000. PMID: 6201849, PMCID: PMC345423, DOI: 10.1073/pnas.81.7.1996.Peer-Reviewed Original ResearchConceptsRibonucleoprotein particleHeLa cellsSmall cytoplasmic RNARibonuclease protection experimentsSmall ribonucleoprotein particlesSmall cytoplasmic ribonucleoproteinsHuman HeLa cellsCytoplasmic ribonucleoproteinMammalian speciesCytoplasmic RNARNA sequencesMajor proteinsRo RNAsProtection experimentsRo proteinPossible functionsBase pairsIdentical base pairsRNAProteinSystemic lupus erythematosusAntigenic proteinsAntigenic polypeptidesRo antibodiesLupus erythematosus
1982
Precursor molecules of both human 5S ribosomal RNA and transfer RNAs are bound by a cellular protein reactive with anti-La Lupus antibodies
Rinke J, Steitz J. Precursor molecules of both human 5S ribosomal RNA and transfer RNAs are bound by a cellular protein reactive with anti-La Lupus antibodies. Cell 1982, 29: 149-159. PMID: 7105180, DOI: 10.1016/0092-8674(82)90099-x.Peer-Reviewed Original ResearchConceptsRRNA moleculesLa proteinLa RNAsPrecursor formNuclear transcription systemUninfected mammalian cellsPulse-chase experimentsSmall RNAsSmall ribonucleoproteinPrecursor moleculesTransfer RNAMammalian cellsRibosomal RNATRNA precursorsCertain tRNAsSpecific tRNAsRNA transcriptsTranscription systemU residuesCell extractsMature sizeHeLa cellsRNAEssential roleProtein