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-Binding ProteinsRNA, MessengerSaccharomyces 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
2000
Human Upf Proteins Target an mRNA for Nonsense-Mediated Decay When Bound Downstream of a Termination Codon
Lykke-Andersen J, Shu M, Steitz J. Human Upf Proteins Target an mRNA for Nonsense-Mediated Decay When Bound Downstream of a Termination Codon. Cell 2000, 103: 1121-1131. PMID: 11163187, DOI: 10.1016/s0092-8674(00)00214-2.Peer-Reviewed Original ResearchConceptsNonsense-mediated decayExon-exon junctionsTermination codonMRNA exon-exon junctionsNovel human proteinTranslation termination siteHeLa cell extractsBeta-globin mRNAPremature termination codonUpf proteinsEukaryotic cellsAberrant mRNAsHuman proteinsTermination sitesIntact cellsCell extractsCodonHUpf2ProteinMRNAHUpf1CellsCytoplasmCytoplasmicTethering
1989
The mammalian analogue of the yeast PRP8 splicing protein is present in the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome.
Pinto AL, Steitz JA. The mammalian analogue of the yeast PRP8 splicing protein is present in the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 8742-8746. PMID: 2479028, PMCID: PMC298364, DOI: 10.1073/pnas.86.22.8742.Peer-Reviewed Original ResearchConceptsSmall nuclear ribonucleoproteinU5 small nuclear ribonucleoproteinHeLa cell nuclear extractsSmall nuclear ribonucleoprotein particleCell nuclear extractsAnti-trimethylguanosine antibodyNuclear ribonucleoprotein particleAffinity-purified spliceosomesSplicing proteinsMammalian proteinsYeast proteinsSnRNP complexMRNA splicingSplicing extractsRibonucleoprotein particleNuclear ribonucleoproteinMammalian analogueNuclear extractsSm classGradient fractionationSm epitopesProteinSpliceosomeProtein reactivePrp8
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