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 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, MessengerRNA-Binding ProteinsSerineTransfectionXenopus
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 componentComplexesCodonSubunitsMachineryA 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
1998
Modification of U6 Spliceosomal RNA Is Guided by Other Small RNAs
Tycowski K, You Z, Graham P, Steitz J. Modification of U6 Spliceosomal RNA Is Guided by Other Small RNAs. Molecular Cell 1998, 2: 629-638. PMID: 9844635, DOI: 10.1016/s1097-2765(00)80161-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCell FractionationCell LineCell NucleolusChromosomal Proteins, Non-HistoneDimerizationHeLa CellsHumansMethylationMiceMolecular Sequence DataNucleic Acid ConformationOligodeoxyribonucleotides, AntisenseOocytesPrecipitin TestsRibonuclease HRNA, Ribosomal, 28SRNA, Small NuclearSpliceosomesXenopus laevis
1992
Three 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
An intact Box C sequence in the U3 snRNA is required for binding of fibrillarin, the protein common to the major family of nucleolar snRNPs.
Baserga SJ, Yang XD, Steitz JA. An intact Box C sequence in the U3 snRNA is required for binding of fibrillarin, the protein common to the major family of nucleolar snRNPs. The EMBO Journal 1991, 10: 2645-51. PMID: 1714385, PMCID: PMC452965, DOI: 10.1002/j.1460-2075.1991.tb07807.x.Peer-Reviewed Original ResearchConceptsBox CU3 snRNANucleolar small RNAsSite-specific mutationsShort nucleotide sequencesFibrillarin proteinSmall RNAsDeletion analysisCommon binding siteBox DNucleotide sequenceSnRNPsMajor familiesSnRNAU3 snRNPRNAInput RNAFibrillarinBinding sitesC sequencesBindingProteinSequenceAnti-fibrillarin autoantibodiesBiogenesis
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
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