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
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 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 reactionsBoth 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 determinants