2019
How Complementary Targets Expose the microRNA 3′ End for Tailing and Trimming during Target-Directed microRNA Degradation
Pawlica P, Sheu-Gruttadauria J, MacRae IJ, Steitz JA. How Complementary Targets Expose the microRNA 3′ End for Tailing and Trimming during Target-Directed microRNA Degradation. Cold Spring Harbor Symposia On Quantitative Biology 2019, 84: 039321. PMID: 32019864, PMCID: PMC9161719, DOI: 10.1101/sqb.2019.84.039321.Peer-Reviewed Original ResearchTarget-directed miRNA degradationMiRNA 3' endCellular enzymesMiRNA seed sequencesMiRNA complementarityMiRNA decayArgonaute proteinsMicroRNA degradationMiRNA degradationMiRNA 5Posttranscriptional regulationMiRNA targetsCertain transcriptsSeed sequenceExtensive complementarityMolecular mechanismsMessenger RNATranscriptsEnzymeRegulationEnzymatic attackRecent advancesTargetMicroRNAsRNA
2014
3′-Biotin-tagged microRNA-27 does not associate with Argonaute proteins in cells
Guo YE, Steitz JA. 3′-Biotin-tagged microRNA-27 does not associate with Argonaute proteins in cells. RNA 2014, 20: 985-988. PMID: 24821854, PMCID: PMC4114695, DOI: 10.1261/rna.045054.114.Peer-Reviewed Original Research
2009
Nuclear networking fashions pre-messenger RNA and primary microRNA transcripts for function
Pawlicki JM, Steitz JA. Nuclear networking fashions pre-messenger RNA and primary microRNA transcripts for function. Trends In Cell Biology 2009, 20: 52-61. PMID: 20004579, PMCID: PMC2821161, DOI: 10.1016/j.tcb.2009.10.004.Peer-Reviewed Original ResearchConceptsMature messenger RNAGene expressionRNA polymerase II transcriptsProtein-coding genesPolymerase II transcriptsRNA polymerase IIMessenger RNAPre-messenger RNARNA processing reactionsCotranscriptional eventsPolymerase IIProcessing eventsProcessing reactionsExtensive molecular interactionsEarly stepsTranscriptsRNAExquisite couplingMolecular interactionsMicroRNAsExpressionNuclear networkCrucial roleFinal fateSplicing
2008
Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′‐end maturation
Kolev NG, Yario TA, Benson E, Steitz JA. Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′‐end maturation. EMBO Reports 2008, 9: 1013-1018. PMID: 18688255, PMCID: PMC2572124, DOI: 10.1038/embor.2008.146.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceBase SequenceCell LineCleavage And Polyadenylation Specificity FactorConserved SequenceEndonucleasesEnzyme ActivationHeLa CellsHistonesHumansMolecular Sequence DataProtein Structure, TertiaryProtein SubunitsRNA 3' End ProcessingRNA PrecursorsRNA, MessengerConceptsPre-messenger RNAPolyadenylation specificity factorMammalian proteinsRNase ZConserved motifsHistone mRNASpecificity factorEndonucleolytic cleavageActive endonucleaseEndonuclease activityMBL familyComplex machineryMessenger RNAPoint mutationsCPSF73CPSF100Process of maturationMaturation processRNAProteinMotifMRNAMaturationEukaryotesCleavage
2005
Symplekin and multiple other polyadenylation factors participate in 3′-end maturation of histone mRNAs
Kolev NG, Steitz JA. Symplekin and multiple other polyadenylation factors participate in 3′-end maturation of histone mRNAs. Genes & Development 2005, 19: 2583-2592. PMID: 16230528, PMCID: PMC1276732, DOI: 10.1101/gad.1371105.Peer-Reviewed Original ResearchConceptsTail elongationU7 small nuclear ribonucleoproteinCommon molecular machineryMammalian cell extractsCleavage stimulation factorPolyadenylation specificity factorSmall nuclear ribonucleoproteinMolecular machineryHistone mRNAProtein complexesMRNA cleavageSpecificity factorPolyadenylation factorsTranslational activationNuclear ribonucleoproteinSymplekinReconstitution experimentsCell extractsHeat-labile factorMessenger RNAHistonesMRNAStimulation factorSubunitsCytoplasmic
2001
Protein ligands mediate the CRM1-dependent export of HuR in response to heat shock.
Gallouzi IE, Brennan CM, Steitz JA. Protein ligands mediate the CRM1-dependent export of HuR in response to heat shock. RNA 2001, 7: 1348-61. PMID: 11565755, PMCID: PMC1370177, DOI: 10.1017/s1355838201016089.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAntigens, SurfaceCarrier ProteinsCytoplasmELAV ProteinsELAV-Like Protein 1Fatty Acids, UnsaturatedHeat-Shock ResponseHeLa CellsHumansKaryopherinsLigandsNeuropeptidesNuclear ProteinsPhosphoproteinsReceptors, Cytoplasmic and NuclearRNA, MessengerRNA-Binding ProteinsConceptsAU-rich elementsNuclear exportHeat shockMessenger RNANuclear export factor CRM1Protein ligandsInhibitor of CRM1Export factor CRM1CRM1-dependent exportMRNA nuclear exportRNA-binding proteinProtein-protein interactionsRapid mRNA turnoverEarly response genesAssociation of HuRHeat shock inducesCytoplasmic fociHnRNP complexesExport pathwayMRNA turnoverLeptomycin BCoimmunoprecipitation experimentsCytoplasmic interactionsNES domainResponse genes
1998
Overexpression of HuR, a nuclear–cytoplasmic shuttling protein, increases the in vivo stability of ARE‐containing mRNAs
Fan X, Steitz J. Overexpression of HuR, a nuclear–cytoplasmic shuttling protein, increases the in vivo stability of ARE‐containing mRNAs. The EMBO Journal 1998, 17: 3448-3460. PMID: 9628880, PMCID: PMC1170681, DOI: 10.1093/emboj/17.12.3448.Peer-Reviewed Original ResearchConceptsAU-rich elementsOverexpression of HuRUntranslated regionRNA recognition motif 3Beta-globin reporter mRNAClass II AU-rich elementsAnti-HuR antibodyMouse L929 cellsMRNA decayELAV familyVivo decay ratesDeletion mutantsReporter mRNAL929 cellsMotif 3HuR functionMRNA stabilityCytoplasmic compartmentRNA sequencesRRMs 3HuR proteinVivo roleMessenger RNAHuRHuR antibody
1997
Identification of HuR as a protein implicated in AUUUA‐mediated mRNA decay
Myer V, Fan X, Steitz J. Identification of HuR as a protein implicated in AUUUA‐mediated mRNA decay. The EMBO Journal 1997, 16: 2130-2139. PMID: 9155038, PMCID: PMC1169815, DOI: 10.1093/emboj/16.8.2130.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsAntigens, SurfaceBase CompositionCell ExtractsCross-Linking ReagentsELAV ProteinsELAV-Like Protein 1Gene Expression RegulationHeLa CellsHumansMiceMolecular Sequence DataMolecular WeightRegulatory Sequences, Nucleic AcidRNA-Binding ProteinsRNA, MessengerUltraviolet RaysConceptsAU-rich elementsMRNA decayUntranslated regionRNA-binding specificityARE-binding proteinsHeLa nuclear extractsGene familyMRNA degradationNuclear extractsEssential signalMessenger RNAProteinSequence's abilityHuRAUUUARapid degradationCritical roleHuR.RNAMachineryMRNADegradationRegulationSubsequent analysisExpression
1996
Length suppression in histone messenger RNA 3′-end maturation: Processing defects of insertion mutant premessenger RNAs can be compensated by insertions into the U7 small nuclear RNA
Scharl E, Steitz J. Length suppression in histone messenger RNA 3′-end maturation: Processing defects of insertion mutant premessenger RNAs can be compensated by insertions into the U7 small nuclear RNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 14659-14664. PMID: 8962110, PMCID: PMC26191, DOI: 10.1073/pnas.93.25.14659.Peer-Reviewed Original ResearchConceptsHistone downstream elementU7 RNAHistone messenger RNASmall nuclear RNARNA processing systemSmall ribonucleoproteinPremessenger RNANuclear RNAPre-mRNAU7 small nuclear RNADownstream elementsCleavage siteRNAMessenger RNAXenopus oocytesBase pairingProcessing defectsU7First demonstrationHistonesRNAsRibonucleoproteinInsertionMRNASites
1994
The site of 3′ end formation of histone messenger RNA is a fixed distance from the downstream element recognized by the U7 snRNP.
Scharl EC, Steitz JA. The site of 3′ end formation of histone messenger RNA is a fixed distance from the downstream element recognized by the U7 snRNP. The EMBO Journal 1994, 13: 2432-2440. PMID: 8194533, PMCID: PMC395109, DOI: 10.1002/j.1460-2075.1994.tb06528.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCell NucleusCell-Free SystemCross-Linking ReagentsFurocoumarinsGuanosineHeLa CellsHistonesHumansMiceMolecular Sequence DataNucleic Acid ConformationProtein BindingRegulatory Sequences, Nucleic AcidRibonuclease HRibonucleoproteins, Small NuclearRNA Processing, Post-TranscriptionalRNA, MessengerStructure-Activity RelationshipSubstrate SpecificityConceptsHistone downstream elementU7 small nuclear ribonucleoproteinSmall nuclear ribonucleoproteinHistone messenger RNAInsertion mutantsEnd formationSite of cleavageEnd processingDownstream elementsA residuesMessenger RNAAnti-trimethylguanosine antibodyStem-loop structureWild-type substrateCross-linking studiesPremessenger RNANuclear ribonucleoproteinEnzymatic componentsNew cleavage siteNucleotides downstreamC residuesMolecular rulerCleavage siteRNAHistones
1992
Interactions of Small Nuclear RNA's with Precursor Messenger RNA During in Vitro Splicing
Wassarman D, Steitz J. Interactions of Small Nuclear RNA's with Precursor Messenger RNA During in Vitro Splicing. Science 1992, 257: 1918-1925. PMID: 1411506, DOI: 10.1126/science.1411506.Peer-Reviewed Original ResearchConceptsPrecursor messenger RNASmall nuclear RNANuclear RNASplice siteMessenger RNAPrecursor messenger RNA splicingU6 small nuclear RNAMessenger RNA splicingHeLa nuclear extractsExcised lariat intronSmall RNAsRNA splicingLariat intronIntron sequencesVitro splicingNuclear extractsCleavage eventsSplicingRNAU5Branch siteFirst cleavage eventU6U2U1
1988
snRNP mediators of 3′ end processing: functional fossils?
Mowry K, Steitz J. snRNP mediators of 3′ end processing: functional fossils? Trends In Biochemical Sciences 1988, 13: 447-451. PMID: 2908086, DOI: 10.1016/0968-0004(88)90220-4.Peer-Reviewed Original ResearchConceptsGene expression apparatusMRNA 3' end formationHistone mRNA 3' end formationEukaryotic messenger RNAsRNA processing reactionsRNA recognitionEnd formationRNA moleculesEnd processingProcessing reactionsBase pairsEarly evolutionMessenger RNASnRNPsCurrent understandingMajor playersPolyadenylationSplicingRNAFossilsSequenceMaturationMediators
1987
Identification of the Human U7 snRNP as One of Several Factors Involved in the 3′ End Maturation of Histone Premessenger RNA's
Mowry K, Steitz J. Identification of the Human U7 snRNP as One of Several Factors Involved in the 3′ End Maturation of Histone Premessenger RNA's. Science 1987, 238: 1682-1687. PMID: 2825355, DOI: 10.1126/science.2825355.Peer-Reviewed Original ResearchConceptsU7 snRNPPre-mRNAEnd processingDownstream elementsCleavage siteSmall nuclear ribonucleoprotein complexesMammalian pre-mRNAHeLa cell extractsNuclear ribonucleoprotein complexesHistone pre-mRNAEnd maturationEukaryotic cellsRibonucleoprotein complexesPremessenger RNARNA moietySplicing reactionGene transcriptsCell extractsSnRNPMessenger RNARNA
1979
Genetic Signals and Nucleotide Sequences in Messenger RNA
Steitz J. Genetic Signals and Nucleotide Sequences in Messenger RNA. Biological Regulation And Development 1979, 349-399. DOI: 10.1007/978-1-4684-3417-0_9.Peer-Reviewed Original ResearchRNA moleculesMessenger RNAMessenger RNA moleculesAminoacyl-tRNA synthetasesSequence of nucleotidesThree-dimensional foldingSequence of basesGenetic signalsRNA functionRibosomal RNANucleotide sequenceTRNA moleculesGenetic informationU residuesWatson-Crick base pairsTertiary structureBase pairsPolypeptide chainRNABase pairingSpecific recognitionSequenceProteinString of beadsSynthetases
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 studiesMRNAComplexesThe nucleotide sequence of a major glycine transfer RNA from the posterior silk gland of Bombyx mori L.
Zúñiga M, Steitz J. The nucleotide sequence of a major glycine transfer RNA from the posterior silk gland of Bombyx mori L. Nucleic Acids Research 1977, 4: 4175-4196. PMID: 414206, PMCID: PMC343233, DOI: 10.1093/nar/4.12.4175.Peer-Reviewed Original ResearchRNA·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
1974
Nucleotide sequences of the 5′ and 3′ termini of bacteriophage T7 early messenger RNAs synthesized in vivo: Evidence for sequence specificity in RNA processing
Kramer R, Rosenberg M, Steitz J. Nucleotide sequences of the 5′ and 3′ termini of bacteriophage T7 early messenger RNAs synthesized in vivo: Evidence for sequence specificity in RNA processing. Journal Of Molecular Biology 1974, 89: 767-776. PMID: 4449132, DOI: 10.1016/0022-2836(74)90051-5.Peer-Reviewed Original ResearchConceptsEarly regionMessenger RNAAdenylic acid residuesEarly messenger RNATwo-dimensional electrophoretic techniquesLarger precursor moleculeMonocistronic messengerRNA processingGene 0.3RNA speciesNucleotide sequenceSequence specificityAcid residuesMessenger speciesSequence analysisInitiator RNASequence heterogeneityRNAEarly RNATerminusT7 Early messenger RNAs are the direct products of ribonuclease III cleavage
Rosenberg M, Kramer R, Steitz J. T7 Early messenger RNAs are the direct products of ribonuclease III cleavage. Journal Of Molecular Biology 1974, 89: 777-782. PMID: 4615167, DOI: 10.1016/0022-2836(74)90052-7.Peer-Reviewed Original Research
1973
Discriminatory Ribosome Rebinding of Isolated Regions of Protein Synthesis Initiation from the Ribonucleic Acid of Bacteriophage R17
Steitz J. Discriminatory Ribosome Rebinding of Isolated Regions of Protein Synthesis Initiation from the Ribonucleic Acid of Bacteriophage R17. Proceedings Of The National Academy Of Sciences Of The United States Of America 1973, 70: 2605-2609. PMID: 4582190, PMCID: PMC427065, DOI: 10.1073/pnas.70.9.2605.Peer-Reviewed Original ResearchConceptsR17 RNARibosome-binding siteProtein synthesis initiationEscherichia coli ribosomesPolypeptide chain initiationCoat protein regionRibosome bindingBacterial ribosomeRNA moleculesInitiator regionRibosome protectionSynthesis initiationMRNA moleculesInitiator codonColi ribosomesRibosomesNative RNABacteriophage R17Bacillus stearothermophilusRNAMessenger RNARibonucleic acidR17Replicase regionFragments