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
2004
Evidence for reassociation of RNA-binding proteins after cell lysis: Implications for the interpretation of immunoprecipitation analyses
Mili S, Steitz JA. Evidence for reassociation of RNA-binding proteins after cell lysis: Implications for the interpretation of immunoprecipitation analyses. RNA 2004, 10: 1692-1694. PMID: 15388877, PMCID: PMC1370654, DOI: 10.1261/rna.7151404.Peer-Reviewed Original ResearchA 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, MessengerRNA-Binding ProteinsSaccharomyces 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
1989
Function of the mammalian La protein: evidence for its action in transcription termination by RNA polymerase III.
Gottlieb E, Steitz JA. Function of the mammalian La protein: evidence for its action in transcription termination by RNA polymerase III. The EMBO Journal 1989, 8: 851-861. PMID: 2470590, PMCID: PMC400884, DOI: 10.1002/j.1460-2075.1989.tb03446.x.Peer-Reviewed Original ResearchConceptsRNA polymerase III transcriptionPolymerase III transcriptionRNA polymerase IIITranscription complexPolymerase IIILa proteinTranscription termination factorFull-length transcriptsTranscription terminationTermination factorRNA productsTranscription intermediatesTranscriptsTranscriptionProteinComplexesPolymeraseRegulatorAbsence
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
1984
U4 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
1977
Characterization of two mRNA · rRNA complexes implicated in the initiation of protein biosynthesis
Steitz J, Steege D. Characterization of two mRNA · rRNA complexes implicated in the initiation of protein biosynthesis. Journal Of Molecular Biology 1977, 114: 545-558. PMID: 335077, DOI: 10.1016/0022-2836(77)90177-2.Peer-Reviewed Original ResearchConceptsProtein biosynthesisEscherichia coli 16 S ribosomal RNAS ribosomal RNABase pair regionNuclease digestion studiesFragment complexAssignment of residuesRibosomal RNARRNA complexLambda PRBacteriophage lambdaMolecular understandingInitiation siteInitiation eventsStrong experimental supportMessenger RNABiosynthesisThermal denaturation studiesDenaturation studiesRNAPR transcriptsPR regionDigestion studiesMRNAComplexesRNA·RNA and Protein·RNA Interactions During the Initiation of Protein Synthesis
STEITZ J, SPRAGUE K, STEEGE D, YUAN R, LAUGHREA M, MOORE P, WAHBA A. RNA·RNA and Protein·RNA Interactions During the Initiation of Protein Synthesis. 1977, 491-508. DOI: 10.1016/b978-0-12-722560-9.50032-9.Peer-Reviewed Original Research