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
2006
Multiple domains of EBER 1, an Epstein-Barr virus noncoding RNA, recruit human ribosomal protein L22
Fok V, Mitton-Fry RM, Grech A, Steitz JA. Multiple domains of EBER 1, an Epstein-Barr virus noncoding RNA, recruit human ribosomal protein L22. RNA 2006, 12: 872-882. PMID: 16556938, PMCID: PMC1440895, DOI: 10.1261/rna.2339606.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCarrier ProteinsCell LineCross-Linking ReagentsElectrophoretic Mobility Shift AssayHerpesvirus 4, HumanHumansIn Vitro TechniquesMaltose-Binding ProteinsNucleic Acid ConformationPlasmidsProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsRibosomal ProteinsRNA-Binding ProteinsRNA, UntranslatedRNA, ViralSequence DeletionTranscription, GeneticTransfectionUltraviolet Rays
2004
Splicing of U12-type introns deposits an exon junction complex competent to induce nonsense-mediated mRNA decay
Hirose T, Shu MD, Steitz JA. Splicing of U12-type introns deposits an exon junction complex competent to induce nonsense-mediated mRNA decay. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 17976-17981. PMID: 15608055, PMCID: PMC539812, DOI: 10.1073/pnas.0408435102.Peer-Reviewed Original ResearchMeSH KeywordsCell LineCell NucleusCodon, NonsenseDNA, ComplementaryEvolution, MolecularExonsGene Expression RegulationHeLa CellsHumansImmunoprecipitationIntronsMutagenesis, Site-DirectedOpen Reading FramesPlasmidsRibonuclease HRibonucleoproteins, Small NuclearRNARNA PrecursorsRNA SplicingRNA, MessengerRNA, Small NuclearSpliceosomesTime FactorsTransfectionConceptsExon junction complexU12-type intronsOpen reading frameNonsense-mediated mRNA decayU12-type spliceosomeNonsense-mediated decaySmall nuclear ribonucleoproteinU2-type spliceosomePremature termination codonEJC assemblyMetazoan cellsMRNA decayEvolutionary ageDownstream functionsIntron removalNuclear ribonucleoproteinReading frameExon junctionsTermination codonJunction complexGene expressionIntron downstreamSpliceosomeIntronsSplicingEvidence 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 Research
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-Binding ProteinsRNA, MessengerSerineTransfectionXenopus
2001
Proximity of the invariant loop of U5 snRNA to the second intron residue during pre‐mRNA splicing
McConnell T, Steitz J. Proximity of the invariant loop of U5 snRNA to the second intron residue during pre‐mRNA splicing. The EMBO Journal 2001, 20: 3577-3586. PMID: 11432844, PMCID: PMC125517, DOI: 10.1093/emboj/20.13.3577.Peer-Reviewed Original ResearchAnimalsAzidesBase SequenceCross-Linking ReagentsEnhancer Elements, GeneticGlobinsIntronsKineticsMammalsModels, MolecularMolecular Sequence DataNucleic Acid ConformationPlasmidsPolymerase Chain ReactionRibonuclease HRibonucleoproteins, Small NuclearRNA PrecursorsRNA SplicingRNA, Small NuclearThionucleotidesA 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 Proteins
1996
A 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
Uncoupling two functions of the U1 small nuclear ribonucleoprotein particle during in vitro splicing.
Seiwert SD, Steitz JA. Uncoupling two functions of the U1 small nuclear ribonucleoprotein particle during in vitro splicing. Molecular And Cellular Biology 1993, 13: 3135-3145. PMID: 7684489, PMCID: PMC359749, DOI: 10.1128/mcb.13.6.3135.Peer-Reviewed Original ResearchMeSH KeywordsAdenoviridaeAnimalsBase SequenceCaenorhabditis elegansCell NucleusExonsHeLa CellsHumansMolecular Sequence DataNucleic Acid ConformationOligodeoxyribonucleotidesPlasmidsRibonucleoprotein, U1 Small NuclearRNARNA SplicingRNA, Small NuclearSequence Homology, Nucleic AcidTranscription, GeneticTrypanosomatinaConceptsSmall nuclear ribonucleoprotein particleU1 small nuclear ribonucleoprotein particleNuclear ribonucleoprotein particleSplice site recognitionU1 snRNASL RNASplice site regionSplicing substrateRibonucleoprotein particleSpliced leader RNA sequencesVitro splicingSplice siteU1 snRNP functionsEssential splicing factorLeader RNA sequencesNative gel analysisSnRNP functionCaenorhabditis elegansSplicing complexesSplicing factorsLeptomonas collosomaSpliceosome assemblyDifferent intronsU1 RNAMethyl oligoribonucleotide
1992
A new interaction between the mouse 5′ external transcribed spacer of pre-rRNA and U3 snRNA detected by psoralen crosslinking
Tyc K, Steitz J. A new interaction between the mouse 5′ external transcribed spacer of pre-rRNA and U3 snRNA detected by psoralen crosslinking. Nucleic Acids Research 1992, 20: 5375-5382. PMID: 1437554, PMCID: PMC334344, DOI: 10.1093/nar/20.20.5375.Peer-Reviewed Original Research
1990
Herpesvirus saimiri U RNAs are expressed and assembled into ribonucleoprotein particles in the absence of other viral genes
Lee SI, Steitz JA. Herpesvirus saimiri U RNAs are expressed and assembled into ribonucleoprotein particles in the absence of other viral genes. Journal Of Virology 1990, 64: 3905-3915. PMID: 2164602, PMCID: PMC249686, DOI: 10.1128/jvi.64.8.3905-3915.1990.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCallitrichinaeCell NucleusCell Transformation, ViralGene ExpressionGenes, ViralHeLa CellsHerpesvirus 2, SaimiriineHumansMolecular Sequence DataNucleic Acid ConformationPlasmidsRestriction MappingRibonucleoproteinsRibonucleoproteins, Small NuclearRNA, Small NuclearT-LymphocytesTransfection
1989
Each of the conserved sequence elements flanking the cleavage site of mammalian histone pre-mRNAs has a distinct role in the 3'-end processing reaction.
Mowry KL, Oh R, Steitz JA. Each of the conserved sequence elements flanking the cleavage site of mammalian histone pre-mRNAs has a distinct role in the 3'-end processing reaction. Molecular And Cellular Biology 1989, 9: 3105-3108. PMID: 2779556, PMCID: PMC362782, DOI: 10.1128/mcb.9.7.3105.Peer-Reviewed Original Research
1988
An in vitro interaction between the human U3 snRNP and 28S rRNA sequences near the α-sarcin site
Parker K, Bruzik J, Steitz J. An in vitro interaction between the human U3 snRNP and 28S rRNA sequences near the α-sarcin site. Nucleic Acids Research 1988, 16: 10493-10509. PMID: 2974535, PMCID: PMC338920, DOI: 10.1093/nar/16.22.10493.Peer-Reviewed Original ResearchAntibodiesBase CompositionBase SequenceEndoribonucleasesFungal ProteinsHeLa CellsHumansMolecular Sequence DataNucleic Acid ConformationPlasmidsProtein Synthesis InhibitorsRibonuclease T1RibonucleoproteinsRibonucleoproteins, Small NuclearRNA PrecursorsRNA, RibosomalRNA, Ribosomal, 28STranscription, Genetic
1987
Multiple interactions between the splicing substrate and small nuclear ribonucleoproteins in spliceosomes.
Chabot B, Steitz JA. Multiple interactions between the splicing substrate and small nuclear ribonucleoproteins in spliceosomes. Molecular And Cellular Biology 1987, 7: 281-293. PMID: 2951586, PMCID: PMC365068, DOI: 10.1128/mcb.7.1.281.Peer-Reviewed Original Research
1985
U2 as well as U1 small nuclear ribonucleoproteins are involved in premessenger RNA splicing
Black D, Chabot B, Steitz J. U2 as well as U1 small nuclear ribonucleoproteins are involved in premessenger RNA splicing. Cell 1985, 42: 737-750. PMID: 2996775, DOI: 10.1016/0092-8674(85)90270-3.Peer-Reviewed Original Research
1979
Transposition of the Escherichia coli insertion element gamma generates a five-base-pair repeat.
Reed RR, Young RA, Steitz JA, Grindley ND, Guyer MS. Transposition of the Escherichia coli insertion element gamma generates a five-base-pair repeat. Proceedings Of The National Academy Of Sciences Of The United States Of America 1979, 76: 4882-4886. PMID: 388421, PMCID: PMC413041, DOI: 10.1073/pnas.76.10.4882.Peer-Reviewed Original Research
1975
F factor-mediated inhibition of bacteriophage T7 growth: Analysis of T7 RNA and protein synthesis In vivo and In vitro using male and female Escherichia coli
Condit RC, Steitz JA. F factor-mediated inhibition of bacteriophage T7 growth: Analysis of T7 RNA and protein synthesis In vivo and In vitro using male and female Escherichia coli. Journal Of Molecular Biology 1975, 98: 31-43. PMID: 1104867, DOI: 10.1016/s0022-2836(75)80099-4.Peer-Reviewed Original ResearchConceptsT7 growthProtein synthesisE. coliPolyacrylamide gel electrophoresisEscherichia coliPhage protein synthesisGel electrophoresisTranslation apparatusT7 proteinsPhage proteinsT7 infectionT7 DNAT7 RNAFaithful synthesisRNA synthesisProteinMale cellsRNAColiTranscriptionSimultaneous inhibitionSpecific modificationsT7InhibitionElectrophoresis