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-Binding ProteinsRNA, MessengerTime FactorsXenopus laevis
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
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
Both 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