2012
Human spliceosomal protein CWC22 plays a role in coupling splicing to exon junction complex deposition and nonsense-mediated decay
Alexandrov A, Colognori D, Shu MD, Steitz JA. Human spliceosomal protein CWC22 plays a role in coupling splicing to exon junction complex deposition and nonsense-mediated decay. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 21313-21318. PMID: 23236153, PMCID: PMC3535618, DOI: 10.1073/pnas.1219725110.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCarrier ProteinsEukaryotic Initiation Factor-4AEukaryotic Initiation Factor-4GExonsGene Knockdown TechniquesHEK293 CellsHeLa CellsHumansMolecular Sequence DataMutationNonsense Mediated mRNA DecayNuclear ProteinsPeptidylprolyl IsomeraseProtein BindingRNA SplicingRNA, MessengerRNA-Binding ProteinsSpliceosomesConceptsExon junction complexEJC depositionMultiprotein exon junction complexNonsense-mediated decay pathwayNonsense-mediated decaySpecific roleEJC assemblyEJC formationComplex eukaryotesDisrupts associationMetazoan mRNAsSpliceosomal proteinsCellular mRNAsHost genesSplicing defectsJunction complexDownstream eventsSplicingNatural substrateDecay pathwaysCWC22Depletion yieldsNMDMutationsMRNA
2011
Human eIF4AIII interacts with an eIF4G-like partner, NOM1, revealing an evolutionarily conserved function outside the exon junction complex
Alexandrov A, Colognori D, Steitz JA. Human eIF4AIII interacts with an eIF4G-like partner, NOM1, revealing an evolutionarily conserved function outside the exon junction complex. Genes & Development 2011, 25: 1078-1090. PMID: 21576267, PMCID: PMC3093123, DOI: 10.1101/gad.2045411.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsDEAD-box RNA HelicasesEukaryotic Initiation Factor-4AEukaryotic Initiation Factor-4GEvolution, MolecularExonsGene DeletionGenetic Complementation TestHumansModels, MolecularMolecular Sequence DataMutationNuclear ProteinsPhenotypeProtein Structure, TertiaryRNA, Ribosomal, 18SRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentConceptsExon junction complexEIF4GJunction complexDEAD-box helicasePre-rRNA processingDirect physical interactionEIF4G complexExtragenic suppressorsBiogenesis defectsLethal phenotypeGrowth defectTranslation initiationHuman orthologEIF4AIIISaccharomyces cerevisiaeHuman cellsNOM1Physical interactionComplex actsG complexX-ray structureMutationsResiduesComplexesOrthologs
2009
Drosophila hnRNP A1 homologs Hrp36/Hrp38 enhance U2-type versus U12-type splicing to regulate alternative splicing of the prospero twintron
Borah S, Wong AC, Steitz JA. Drosophila hnRNP A1 homologs Hrp36/Hrp38 enhance U2-type versus U12-type splicing to regulate alternative splicing of the prospero twintron. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 2577-2582. PMID: 19196985, PMCID: PMC2636732, DOI: 10.1073/pnas.0812826106.Peer-Reviewed Original ResearchConceptsU12-type splicingPurine-rich elementAlternative splicingMRNA undergoes alternative splicingTranscription factor ProsperoU12-type spliceosomeHeterogeneous nuclear ribonucleoprotein A1Undergoes alternative splicingU2-type spliceosomeDrosophila homologDrosophila embryogenesisS2 cellsHnRNP A1TwintronSplicingNeuronal differentiationHrp38SpliceosomeIntronsEmbryogenesisProteinAxonal outgrowthHrp36HnRNPsHomolog
2008
Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′‐end maturation
Kolev NG, Yario TA, Benson E, Steitz JA. Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′‐end maturation. EMBO Reports 2008, 9: 1013-1018. PMID: 18688255, PMCID: PMC2572124, DOI: 10.1038/embor.2008.146.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceBase SequenceCell LineCleavage And Polyadenylation Specificity FactorConserved SequenceEndonucleasesEnzyme ActivationHeLa CellsHistonesHumansMolecular Sequence DataProtein Structure, TertiaryProtein SubunitsRNA 3' End ProcessingRNA PrecursorsRNA, MessengerConceptsPre-messenger RNAPolyadenylation specificity factorMammalian proteinsRNase ZConserved motifsHistone mRNASpecificity factorEndonucleolytic cleavageActive endonucleaseEndonuclease activityMBL familyComplex machineryMessenger RNAPoint mutationsCPSF73CPSF100Process of maturationMaturation processRNAProteinMotifMRNAMaturationEukaryotesCleavage
2005
An embryonic poly(A)-binding protein (ePAB) is expressed in mouse oocytes and early preimplantation embryos
Seli E, Lalioti MD, Flaherty SM, Sakkas D, Terzi N, Steitz JA. An embryonic poly(A)-binding protein (ePAB) is expressed in mouse oocytes and early preimplantation embryos. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 367-372. PMID: 15630085, PMCID: PMC544294, DOI: 10.1073/pnas.0408378102.Peer-Reviewed Original ResearchConceptsZygotic gene activationGene activationEarly embryosSomatic cellsTranslational activationGene expressionEmbryo developmentEarly preimplantation embryo developmentEarly Xenopus developmentEarly preimplantation embryosEight-cell stageEarly embryo developmentPreimplantation embryo developmentTwo-cell embryosCytoplasmic PABPMouse orthologXenopus developmentMammalian oocytesProphase ISomatic tissuesChromosome 2Preimplantation embryosEPABMouse oocytesOne-cell
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
2003
SR Splicing Factors Serve as Adapter Proteins for TAP-Dependent mRNA Export
Huang Y, Gattoni R, Stévenin J, Steitz JA. SR Splicing Factors Serve as Adapter Proteins for TAP-Dependent mRNA Export. Molecular Cell 2003, 11: 837-843. PMID: 12667464, DOI: 10.1016/s1097-2765(03)00089-3.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsArginineBinding, CompetitiveBiological TransportCell NucleusGenes, DominantGlutathione TransferaseModels, BiologicalMolecular Sequence DataNucleocytoplasmic Transport ProteinsOocytesPeptidesPlasmidsPrecipitin TestsProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsRNA, MessengerRNA-Binding ProteinsSerineTransfectionXenopus
2001
Delineation of mRNA Export Pathways by the Use of Cell-Permeable Peptides
Gallouzi I, Steitz J. Delineation of mRNA Export Pathways by the Use of Cell-Permeable Peptides. Science 2001, 294: 1895-1901. PMID: 11729309, DOI: 10.1126/science.1064693.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntennapedia Homeodomain ProteinAntigens, SurfaceBiological TransportCell LineCell Membrane PermeabilityCell NucleusCytoplasmELAV ProteinsELAV-Like Protein 1Genes, fosHeat-Shock ResponseHomeodomain ProteinsHumansKaryopherinsMolecular Sequence DataNeuropeptidesNuclear ProteinsPeptide FragmentsPhosphoproteinsProtein BindingProtein Structure, TertiaryReceptors, Cytoplasmic and NuclearRegulatory Sequences, Nucleic AcidReproducibility of ResultsRNA StabilityRNA-Binding ProteinsRNA, MessengerTetrahydrofolate DehydrogenaseTranscription FactorsConceptsNuclear export signalAU-rich elementsMessenger RNAsAdapter proteinCell-permeable peptideLeucine-rich nuclear export signalReceptor proteinMRNA export pathwayNuclear pore complexExport receptor CRM1Overall cellular distributionSitu hybridization experimentsMRNA exportExport signalNucleocytoplasmic shuttlingPore complexExport pathwayHybridization experimentsProtein ligandsCellular distributionProteinA novel embryonic poly(A) binding protein, ePAB, regulates mRNA deadenylation in Xenopus egg extracts
Voeltz GK, Ongkasuwan J, Standart N, Steitz JA. A novel embryonic poly(A) binding protein, ePAB, regulates mRNA deadenylation in Xenopus egg extracts. Genes & Development 2001, 15: 774-788. PMID: 11274061, PMCID: PMC312653, DOI: 10.1101/gad.872201.Peer-Reviewed Original ResearchAdenosine MonophosphateAmino Acid SequenceAnimalsBase SequenceBlotting, WesternDNA MethylationGene Expression Regulation, DevelopmentalKineticsMolecular Sequence DataOocytesPlasmidsPoly APoly(A)-Binding ProteinsPrecipitin TestsProtein BindingRecombinant ProteinsRNA-Binding ProteinsSequence Analysis, DNASequence Homology, Amino AcidTime FactorsTranscriptional ActivationUltraviolet RaysXenopusXenopus ProteinsHuR 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
2000
Protein Ligands to Hur Modulate Its Interaction with Target Mrnas in Vivo
Brennan C, Gallouzi I, Steitz J. Protein Ligands to Hur Modulate Its Interaction with Target Mrnas in Vivo. Journal Of Cell Biology 2000, 151: 1-14. PMID: 11018049, PMCID: PMC2189805, DOI: 10.1083/jcb.151.1.1.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAmino Acid SequenceAntigens, SurfaceBinding SitesCarrier ProteinsChromatography, AffinityCytoplasmELAV ProteinsELAV-Like Protein 1Fatty Acids, UnsaturatedHeLa CellsHumansKaryopherinsLigandsMolecular Sequence DataNeuropeptidesNuclear ProteinsPhosphoprotein PhosphatasesPhosphoproteinsProtein BindingProtein Phosphatase 2Protein TransportReceptors, Cytoplasmic and NuclearRNA StabilityRNA-Binding ProteinsRNA, MessengerSequence Analysis, ProteinConceptsAU-rich elementsTarget mRNAsStability of ARENuclear export factor CRM1Protein phosphatase 2A inhibitorExport factor CRM1Phosphatase 2A inhibitorCOOH-terminal tailInhibition of CRM1Leucine-rich repeatsC-fos geneMammalian proteinsLeptomycin BELAV familyCellular mRNAsNuclear retentionSecond motifHuR associationUntranslated regionBind regionsCytoplasmic distributionPp32Protein ligandsCRM1Terminal region
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, MessengerRNA-Binding ProteinsSequence 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 transportMRNA
1997
Inhibition of mammalian spliceosome assembly and pre-mRNA splicing by peptide inhibitors of protein kinases.
Parker AR, Steitz JA. Inhibition of mammalian spliceosome assembly and pre-mRNA splicing by peptide inhibitors of protein kinases. RNA 1997, 3: 1301-12. PMID: 9409621, PMCID: PMC1369569.Peer-Reviewed Original ResearchConceptsCalmodulin binding domainMammalian spliceosome assemblySpliceosome assemblyMRNA splicingSplicing activityCaMK IIGS peptideProtein kinase CAutophosphorylation eventsCalmodulin kinase IIProlonged incubationProtein kinaseSplicing reactionSplicing assaysBinding domainsKinase IISplicingKinase CPeptide inhibitorDistinct mechanismsProteinKinaseCompetitive inhibitorAssemblyDistinct eventsIdentification of HuR as a protein implicated in AUUUA‐mediated mRNA decay
Myer V, Fan X, Steitz J. Identification of HuR as a protein implicated in AUUUA‐mediated mRNA decay. The EMBO Journal 1997, 16: 2130-2139. PMID: 9155038, PMCID: PMC1169815, DOI: 10.1093/emboj/16.8.2130.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsAntigens, SurfaceBase CompositionCell ExtractsCross-Linking ReagentsELAV ProteinsELAV-Like Protein 1Gene Expression RegulationHeLa CellsHumansMiceMolecular Sequence DataMolecular WeightRegulatory Sequences, Nucleic AcidRNA-Binding ProteinsRNA, MessengerUltraviolet RaysConceptsAU-rich elementsMRNA decayUntranslated regionRNA-binding specificityARE-binding proteinsHeLa nuclear extractsGene familyMRNA degradationNuclear extractsEssential signalMessenger RNAProteinSequence's abilityHuRAUUUARapid degradationCritical roleHuR.RNAMachineryMRNADegradationRegulationSubsequent analysisExpression
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
1991
EAP, a highly conserved cellular protein associated with Epstein‐Barr virus small RNAs (EBERs).
Toczyski DP, Steitz JA. EAP, a highly conserved cellular protein associated with Epstein‐Barr virus small RNAs (EBERs). The EMBO Journal 1991, 10: 459-466. PMID: 1846807, PMCID: PMC452667, DOI: 10.1002/j.1460-2075.1991.tb07968.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceB-LymphocytesBase SequenceCell LineCell Transformation, ViralCloning, MolecularDNAHerpesvirus 4, HumanHumansMolecular Sequence DataPolymerase Chain ReactionProteinsRibonucleoproteinsRibonucleoproteins, Small NuclearRibosomal ProteinsRNA-Binding ProteinsRNA, Small NuclearRNA, ViralSequence Homology, Nucleic AcidAlive with DEAD proteins
Wassarman D, Steitz J. Alive with DEAD proteins. Nature 1991, 349: 463-464. PMID: 1825133, DOI: 10.1038/349463a0.Peer-Reviewed Original Research
1987
Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly.
Rich BE, Steitz JA. Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly. Molecular And Cellular Biology 1987, 7: 4065-4074. PMID: 3323886, PMCID: PMC368077, DOI: 10.1128/mcb.7.11.4065.Peer-Reviewed Original ResearchConceptsL7/L12
1982
Nucleotide sequence of γδ resolvase gene and demonstration that its gene product acts as a repressor of transcription
Reed R, Shibuya G, Steitz J. Nucleotide sequence of γδ resolvase gene and demonstration that its gene product acts as a repressor of transcription. Nature 1982, 300: 381-383. PMID: 6292730, DOI: 10.1038/300381a0.Peer-Reviewed Original ResearchConceptsRepressor of transcriptionSite-specific recombination systemResolvase proteinAmino acid sequenceSite-specific recombinationElement-encoded proteinsIntercistronic regionGene initiatesFrequency of transpositionGene productsNucleotide sequenceAcid sequenceRecombination systemTranscription systemGenetic analysisΓδ resolvaseResolvaseGenesTranscriptionProteinResolvase geneRelated transposonsTransposaseModel substrateRecombination
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