2015
The host Integrator complex acts in transcription-independent maturation of herpesvirus microRNA 3′ ends
Xie M, Zhang W, Shu MD, Xu A, Lenis DA, DiMaio D, Steitz JA. The host Integrator complex acts in transcription-independent maturation of herpesvirus microRNA 3′ ends. Genes & Development 2015, 29: 1552-1564. PMID: 26220997, PMCID: PMC4526738, DOI: 10.1101/gad.266973.115.Peer-Reviewed Original ResearchConceptsEnd processing signalsSmall nuclear RNAProximity ligation assayEnd processingPre-miRNAsHerpesvirus saimiriPre-miRNA hairpinsRNA-protein interactionsSitu proximity ligation assayIntegrator complexMiRNA 3MiRNA biogenesisSnRNA 3Primary miRNAMiRNA hairpinsIntegrator activityNuclear RNASequence downstreamOncogenic γ-herpesvirusesRescue experimentsLigation assayVivo knockdownComplex actsΓ-herpesvirusesHairpin
2014
Versatile microRNA biogenesis in animals and their viruses
Xie M, Steitz JA. Versatile microRNA biogenesis in animals and their viruses. RNA Biology 2014, 11: 673-681. PMID: 24823351, PMCID: PMC4156499, DOI: 10.4161/rna.28985.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsMicroRNAsRibonuclease IIIRNA CapsRNA PrecursorsRNA Processing, Post-TranscriptionalTranscription, GeneticVirusesConceptsEssential cellular processesMiRNA regulatory networkPost-transcriptional levelUbiquitous gene regulatorsNon-canonical pathwayMost miRNAsCytoplasmic DicerMicroRNA biogenesisMolecular machineryCellular processesRegulatory networksPrimary transcriptGene regulatorsNuclear DroshaCellular RNABiogenesisDroshaAlternative mechanismFundamental roleCleavage stepMetazoansDicerMiRNAsMicroRNAsMiRNA
2012
Tri-snRNP-associated proteins interact with subunits of the TRAMP and nuclear exosome complexes, linking RNA decay and pre-mRNA splicing
Nag A, Steitz JA. Tri-snRNP-associated proteins interact with subunits of the TRAMP and nuclear exosome complexes, linking RNA decay and pre-mRNA splicing. RNA Biology 2012, 9: 334-342. PMID: 22336707, PMCID: PMC3384585, DOI: 10.4161/rna.19431.Peer-Reviewed Original ResearchConceptsDecay machineryMRNA splicingRNA decay machineryRNA decay factorsTri-snRNP complexNuclear exosome complexPM/SclYeast counterpartIntergenic transcriptsSnoRNA biogenesisExosome complexTri-snRNPRNA decayRRNA processingPhosphorylation sitesMRNA processingPutative componentsMtr4Prp31MachinerySplicingDifferent pathwaysProteinSpliceosomeBiogenesis
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 ResearchMeSH KeywordsAnimalsCell NucleusGene Regulatory NetworksHumansMicroRNAsRNA PrecursorsRNA SplicingTranscription, GeneticConceptsMature 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 processRNAProteinMotifMRNAMaturationEukaryotesCleavageWhere in the cell is the minor spliceosome?
Steitz JA, Dreyfuss G, Krainer AR, Lamond AI, Matera AG, Padgett RA. Where in the cell is the minor spliceosome? Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 8485-8486. PMID: 18562285, PMCID: PMC2438384, DOI: 10.1073/pnas.0804024105.Peer-Reviewed Original Research
2007
U2 snRNP Binds Intronless Histone Pre-mRNAs to Facilitate U7-snRNP-Dependent 3′ End Formation
Friend K, Lovejoy AF, Steitz JA. U2 snRNP Binds Intronless Histone Pre-mRNAs to Facilitate U7-snRNP-Dependent 3′ End Formation. Molecular Cell 2007, 28: 240-252. PMID: 17964263, PMCID: PMC2149891, DOI: 10.1016/j.molcel.2007.09.026.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCell NucleusDEAD-box RNA HelicasesHeLa CellsHistonesHumansIntronsMiceModels, MolecularOocytesProtein ConformationRibonucleoprotein, U2 Small NuclearRibonucleoprotein, U7 Small NuclearRibonucleoproteins, Small NuclearRNA 3' End ProcessingRNA PrecursorsRNA, MessengerRNA-Binding ProteinsTime FactorsXenopus laevis
2006
A Spliceosomal Intron Binding Protein, IBP160, Links Position-Dependent Assembly of Intron-Encoded Box C/D snoRNP to Pre-mRNA Splicing
Hirose T, Ideue T, Nagai M, Hagiwara M, Shu MD, Steitz JA. A Spliceosomal Intron Binding Protein, IBP160, Links Position-Dependent Assembly of Intron-Encoded Box C/D snoRNP to Pre-mRNA Splicing. Molecular Cell 2006, 23: 673-684. PMID: 16949364, DOI: 10.1016/j.molcel.2006.07.011.Peer-Reviewed Original ResearchIn vivo assembly of functional U7 snRNP requires RNA backbone flexibility within the Sm-binding site
Kolev NG, Steitz JA. In vivo assembly of functional U7 snRNP requires RNA backbone flexibility within the Sm-binding site. Nature Structural & Molecular Biology 2006, 13: 347-353. PMID: 16547514, DOI: 10.1038/nsmb1075.Peer-Reviewed Original Research
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 factorSubunitsCytoplasmicSRprises along a Messenger’s Journey
Huang Y, Steitz JA. SRprises along a Messenger’s Journey. Molecular Cell 2005, 17: 613-615. PMID: 15749011, DOI: 10.1016/j.molcel.2005.02.020.Peer-Reviewed Original Research
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 downstreamSpliceosomeIntronsSplicingPremature termination codons do not affect the rate of splicing of neighboring introns
Lytle JR, Steitz JA. Premature termination codons do not affect the rate of splicing of neighboring introns. RNA 2004, 10: 657-668. PMID: 15037775, PMCID: PMC1370556, DOI: 10.1261/rna.5241404.Peer-Reviewed Original Research
2002
The Divergent U12-Type Spliceosome Is Required for Pre-mRNA Splicing and Is Essential for Development in Drosophila
Otake LR, Scamborova P, Hashimoto C, Steitz JA. The Divergent U12-Type Spliceosome Is Required for Pre-mRNA Splicing and Is Essential for Development in Drosophila. Molecular Cell 2002, 9: 439-446. PMID: 11864616, DOI: 10.1016/s1097-2765(02)00441-0.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAnimalsAnimals, Genetically ModifiedBase SequenceDrosophila melanogasterDrosophila ProteinsGenes, LethalIntronsLarvaMolecular Sequence DataMutagenesis, InsertionalNerve Tissue ProteinsNuclear ProteinsNucleic Acid ConformationProtein IsoformsRibonucleoprotein, U4-U6 Small NuclearRibonucleoproteins, Small NuclearRNA PrecursorsRNA SplicingRNA, Small NuclearSequence AlignmentSequence Homology, Nucleic AcidSpliceosomesTranscription FactorsTransgenesConceptsU12-type spliceosomeThird instar larvalU12-type intronsPre-mRNA splicingU4atac/U6atacMetazoan organismsHomeodomain proteinsU5 snRNPsDrosophila melanogasterU12 spliceosomeMRNA intronsU12 snRNASingle locusU6atacInstar larvalSpliceosomeEmbryonic stagesCNS developmentIntronsMinor classU12DrosophilaMelanogasterVertebratesSnRNPs
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 NuclearThionucleotides
1999
Guided tours: from precursor snoRNA to functional snoRNP
Weinstein L, Steitz J. Guided tours: from precursor snoRNA to functional snoRNP. Current Opinion In Cell Biology 1999, 11: 378-384. PMID: 10395551, DOI: 10.1016/s0955-0674(99)80053-2.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell NucleolusHumansRibonucleoproteins, Small NuclearRNA PrecursorsRNA, Small NuclearTranscription, Genetic
1997
Inhibition of mammalian spliceosome assembly and pre-mRNA splicing by peptide inhibitors of protein kinases.
Parker AR, Steitz JA. Inhibition of mammalian spliceosome assembly and pre-mRNA splicing by peptide inhibitors of protein kinases. RNA 1997, 3: 1301-12. PMID: 9409621, PMCID: PMC1369569.Peer-Reviewed Original ResearchConceptsCalmodulin binding domainMammalian spliceosome assemblySpliceosome assemblyMRNA splicingSplicing activityCaMK IIGS peptideProtein kinase CAutophosphorylation eventsCalmodulin kinase IIProlonged incubationProtein kinaseSplicing reactionSplicing assaysBinding domainsKinase IISplicingKinase CPeptide inhibitorDistinct mechanismsProteinKinaseCompetitive inhibitorAssemblyDistinct eventsPre-mRNA splicing: the discovery of a new spliceosome doubles the challenge
Tarn W, Steitz J. Pre-mRNA splicing: the discovery of a new spliceosome doubles the challenge. Trends In Biochemical Sciences 1997, 22: 132-137. PMID: 9149533, DOI: 10.1016/s0968-0004(97)01018-9.Peer-Reviewed Original Research
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 demonstrationHistonesRNAsRibonucleoproteinInsertionMRNASitesHighly Diverged U4 and U6 Small Nuclear RNAs Required for Splicing Rare AT-AC Introns
Tarn W, Steitz J. Highly Diverged U4 and U6 Small Nuclear RNAs Required for Splicing Rare AT-AC Introns. Science 1996, 273: 1824-1832. PMID: 8791582, DOI: 10.1126/science.273.5283.1824.Peer-Reviewed Original Research