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
2004
An Intronic Enhancer Regulates Splicing of the Twintron of Drosophila melanogaster prospero Pre-mRNA by Two Different Spliceosomes
Scamborova P, Wong A, Steitz JA. An Intronic Enhancer Regulates Splicing of the Twintron of Drosophila melanogaster prospero Pre-mRNA by Two Different Spliceosomes. Molecular And Cellular Biology 2004, 24: 1855-1869. PMID: 14966268, PMCID: PMC350559, DOI: 10.1128/mcb.24.5.1855-1869.2004.Peer-Reviewed Original ResearchConceptsPurine-rich elementSplicing pathwaySplice siteU12-type spliceosomeU12-type splicingVitro splicing systemForms of mRNAAlternative splicingEarly embryogenesisKc cellsIntron sequencesPre-mRNASystematic deletionIntronic enhancerSplicingSequence requirementsIntron regionsEnhancer elementsNucleotides downstreamMolecular mechanismsTwintronSpliceosomeSplicing systemMutation analysisPathway
1997
A new strategy for introducing photoactivatable 4-thiouridine ((4S)U) into specific positions in a long RNA molecule.
Yu YT, Steitz JA. A new strategy for introducing photoactivatable 4-thiouridine ((4S)U) into specific positions in a long RNA molecule. RNA 1997, 3: 807-10. PMID: 9214662, PMCID: PMC1369526.Peer-Reviewed Original ResearchConceptsPre-mRNAPre-mRNA substrateAT-AC intronsPhage RNA polymeraseRNA-DNA chimerasFull-length RNALong RNA moleculesRNA polymeraseRNA moleculesT4 RNA ligaseT4 DNA ligaseRNA ligaseDNA ligaseRNARNase H cleavageLigaseSpecific sitesSpecific positionsIntronsPolymeraseChimerasNew strategyCleavageOligonucleotideH cleavage
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 demonstrationHistonesRNAsRibonucleoproteinInsertionMRNASitesA Novel Spliceosome Containing U11, U12, and U5 snRNPs Excises a Minor Class (AT–AC) Intron In Vitro
Tarn W, Steitz J. A Novel Spliceosome Containing U11, U12, and U5 snRNPs Excises a Minor Class (AT–AC) Intron In Vitro. Cell 1996, 84: 801-811. PMID: 8625417, DOI: 10.1016/s0092-8674(00)81057-0.Peer-Reviewed Original ResearchMeSH KeywordsBase CompositionBase SequenceBlotting, NorthernCell NucleusHeLa CellsHumansMolecular Sequence DataNucleic Acid ConformationOligodeoxyribonucleotidesPlasmidsPolymerase Chain ReactionRibonuclease HRibonucleoprotein, U5 Small NuclearRibonucleoproteins, Small NuclearRNA PrecursorsRNA SplicingConceptsU5 small nuclear ribonucleoproteinSmall nuclear ribonucleoproteinU12 small nuclear ribonucleoproteinsMinor class intronsProtein coding genesPre-mRNA substrateNative gel electrophoresisCoding genesBranch site sequenceSplicing complexesNuclear ribonucleoproteinPre-mRNAP120 geneLariat intermediateSite sequenceIntronsHeLa cellsEssential roleSplicingGel electrophoresisBranch siteGenesU12Minor classU11
1993
The U5 and U6 Small Nuclear RNAs as Active Site Components of the Spliceosome
Sontheimer E, Steitz J. The U5 and U6 Small Nuclear RNAs as Active Site Components of the Spliceosome. Science 1993, 262: 1989-1996. PMID: 8266094, DOI: 10.1126/science.8266094.Peer-Reviewed Original ResearchConceptsSmall nuclear RNANuclear RNAPrecursor messenger RNA splicingLariat intermediateU6 small nuclear RNAMessenger RNA splicingExon 1Self-splicing intronsActive site componentsRNA splicingMammalian spliceosomeU6 RNARNA contactsMechanistic parallelsPre-mRNAVitro splicingSubsequent splicingSplicingSpliceosomeSplice siteLast residueFirst residueFunctional interactionIntron productsRNA
1992
Site-specific cross-linking of mammalian U5 snRNP to the 5' splice site before the first step of pre-mRNA splicing.
Wyatt JR, Sontheimer EJ, Steitz JA. Site-specific cross-linking of mammalian U5 snRNP to the 5' splice site before the first step of pre-mRNA splicing. Genes & Development 1992, 6: 2542-2553. PMID: 1340469, DOI: 10.1101/gad.6.12b.2542.Peer-Reviewed Original ResearchConceptsSplice siteMRNA splicingATP-dependent interactionHeLa nuclear extractsU5 snRNPMRNA substratesSplice site regionProtein factorsU5 snRNANucleotides upstreamU6 snRNAPre-mRNANuclear extractsSplicingSite regionLoop sequenceCross-link formationSnRNASplicing conditionsWatson-Crick complementarityCross-linking strategyU1Selective photoactivationSnRNPMammalian
1991
Multiple processing-defective mutations in a mammalian histone pre-mRNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro.
Bond UM, Yario TA, Steitz JA. Multiple processing-defective mutations in a mammalian histone pre-mRNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro. Genes & Development 1991, 5: 1709-1722. PMID: 1885007, DOI: 10.1101/gad.5.9.1709.Peer-Reviewed Original ResearchConceptsHistone downstream elementHistone pre-mRNAMammalian histone pre-mRNAsPre-mRNAHeLa cellsBase pair regionMammalian histonesU7 geneSm snRNPsU7 snRNPGenetic evidenceU7 snRNAUnexpected toleranceU7 RNANuclear extractsDownstream elementsSuppressor geneCompensatory changesGenesBlock substitutionsRNAVivoSnRNPsSnRNPCells
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 RNARNABoth Conserved Signals on Mammalian Histone Pre-mRNAs Associate with Small Nuclear Ribonucleoproteins During 3′ end Formation in Vitro
Mowry K, Steitz J. Both Conserved Signals on Mammalian Histone Pre-mRNAs Associate with Small Nuclear Ribonucleoproteins During 3′ end Formation in Vitro. Molecular And Cellular Biology 1987, 7: 1663-1672. DOI: 10.1128/mcb.7.5.1663-1672.1987.Peer-Reviewed Original ResearchSmall nuclear ribonucleoproteinEnd formationNuclear ribonucleoproteinSequence elementsSm small nuclear ribonucleoproteinsMouse histone genesHeLa cell nuclear extractsHistone H3 transcriptsHuman histone H3Trimethylguanosine cap structureCell nuclear extractsHistone pre-mRNAHairpin loop structureH3 transcriptsHistone genesConserved signalU RNAHistone H3MRNA substratesPre-mRNACap structureNuclear extractsRNA fragmentsProcessing reactionsProtein determinantsBoth conserved signals on mammalian histone pre-mRNAs associate with small nuclear ribonucleoproteins during 3' end formation in vitro.
Mowry KL, Steitz JA. Both conserved signals on mammalian histone pre-mRNAs associate with small nuclear ribonucleoproteins during 3' end formation in vitro. Molecular And Cellular Biology 1987, 7: 1663-1672. PMID: 2955216, PMCID: PMC365266, DOI: 10.1128/mcb.7.5.1663.Peer-Reviewed Original ResearchConceptsSmall nuclear ribonucleoproteinEnd formationNuclear ribonucleoproteinSequence elementsSm small nuclear ribonucleoproteinsMouse histone genesHeLa cell nuclear extractsHistone H3 transcriptsHuman histone H3Trimethylguanosine cap structureCell nuclear extractsHistone pre-mRNAHairpin loop structureH3 transcriptsHistone genesMammalian histonesU RNAHistone H3MRNA substratesPre-mRNACap structureMRNA associatesNuclear extractsRNA fragmentsProcessing reactions