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
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