2009
A Conserved WD40 Protein Binds the Cajal Body Localization Signal of scaRNP Particles
Tycowski KT, Shu MD, Kukoyi A, Steitz JA. A Conserved WD40 Protein Binds the Cajal Body Localization Signal of scaRNP Particles. Molecular Cell 2009, 34: 47-57. PMID: 19285445, PMCID: PMC2700737, DOI: 10.1016/j.molcel.2009.02.020.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAnimalsBase SequenceCell LineChromatography, AffinityCoiled BodiesDrosophila melanogasterDrosophila ProteinsHeLa CellsHumansMolecular Sequence DataNucleic Acid ConformationRecombinant Fusion ProteinsRegulatory Sequences, Ribonucleic AcidRibonucleoproteinsRNA-Binding ProteinsSequence AlignmentConceptsCAB boxCB localizationSmall Cajal bodyWD40 proteinsRNP functionCajal bodiesLocalization signalACA motifDomain RNATelomerase RNAHuman homologPosttranscriptional modificationsSmall nuclearWDR79ScaRNAsRNA elementsCentral playerUV crosslinkNuclear RNPCore proteinRNAProteinAdditional interactionsBindingLocalization
2007
AU-Rich-Element-Mediated Upregulation of Translation by FXR1 and Argonaute 2
Vasudevan S, Steitz JA. AU-Rich-Element-Mediated Upregulation of Translation by FXR1 and Argonaute 2. Cell 2007, 128: 1105-1118. PMID: 17382880, PMCID: PMC3430382, DOI: 10.1016/j.cell.2007.01.038.Peer-Reviewed Original ResearchMeSH Keywords3' Untranslated RegionsArgonaute ProteinsCell CycleCell LineChromatography, AffinityCulture Media, Serum-FreeEukaryotic Initiation Factor-2Genes, ReporterHumansLuciferases, FireflyMonocytesPeptide Initiation FactorsPolyribosomesProtein BiosynthesisRegulatory Sequences, Ribonucleic AcidRibonucleoproteinsRNA-Binding ProteinsSerumTumor Necrosis Factor-alphaUp-RegulationConceptsAU-rich elementsArgonaute 2Posttranscriptional regulatory systemsAffinity purification methodShRNA knockdown experimentsCell cycle arrestHuman cell linesTranslation activationRegulatory signalsMRNA stabilityGene expressionSerum starvationAU-RichFXR1Activation roleRegulatory systemProtein 1Cell linesMRNA levelsNew insightsDevelopmental consequencesTranslation conditionsUpregulationDirect evidencePurification method
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
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
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