SR proteins can compensate for the loss of U1 snRNP functions in vitro.
Tarn WY, Steitz JA. SR proteins can compensate for the loss of U1 snRNP functions in vitro. Genes & Development 1994, 8: 2704-2717. PMID: 7958927, DOI: 10.1101/gad.8.22.2704.Peer-Reviewed Original ResearchConceptsSR proteinsSplice site recognitionSplice siteU1 snRNPsU1 snRNP functionsEssential splicing factorPre-mRNA substrateSplice site choiceNative gel analysisSplice site selectionMethyl oligoribonucleotideCross-linking studiesSnRNP functionSplicing factorsU1 snRNPU1 snRNASite recognitionSite choiceGel analysisRescue splicingProteinSplicing systemIntronsSnRNPsThe 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