2017
An Exportin-1–dependent microRNA biogenesis pathway during human cell quiescence
Martinez I, Hayes KE, Barr JA, Harold AD, Xie M, Bukhari SIA, Vasudevan S, Steitz JA, DiMaio D. An Exportin-1–dependent microRNA biogenesis pathway during human cell quiescence. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: e4961-e4970. PMID: 28584122, PMCID: PMC5488920, DOI: 10.1073/pnas.1618732114.Peer-Reviewed Original ResearchConceptsBiogenesis pathwayExportin 1Exportin-5Canonical miRNA biogenesis pathwayCanonical miRNA biogenesisTrimethylguanosine synthase 1MicroRNA biogenesis pathwayMiRNA biogenesis pathwayMiRNA processing pathwayStem cell biologyCellular growth arrestGroup of miRNAsExpression of miRNAsPrimary human fibroblastsMiRNA biogenesisPrimary miRNAsCellular quiescenceTissue homeostasisCell biologyProliferative arrestSpecific miRNAsCell quiescenceGrowth arrestBiogenesisMiRNAs
2013
Mammalian 5′-Capped MicroRNA Precursors that Generate a Single MicroRNA
Xie M, Li M, Vilborg A, Lee N, Shu MD, Yartseva V, Šestan N, Steitz JA. Mammalian 5′-Capped MicroRNA Precursors that Generate a Single MicroRNA. Cell 2013, 155: 1568-1580. PMID: 24360278, PMCID: PMC3899828, DOI: 10.1016/j.cell.2013.11.027.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsArgonaute ProteinsBase SequenceBiosynthetic PathwaysDEAD-box RNA HelicasesGenome-Wide Association StudyGuanosineHumansKaryopherinsMiceMicroRNAsMolecular Sequence DataReceptors, Cytoplasmic and NuclearRibonuclease IIIRNA CapsRNA Polymerase IIRNA, Small InterferingTranscription Termination, GeneticConceptsCap-binding protein eIF4EMiRNA biogenesis pathwayNuclear-cytoplasmic transportGuide strand selectionShRNA expression constructsTranscription start siteBiogenesis pathwayCytoplasmic DicerMicroprocessor complexTranscription terminationProtein eIF4EExportin-5MicroRNA precursorsMiRNA hairpinsPrimary transcriptStrand selectionGene regulatorsStart siteDicer cleavageExpression constructsSingle microRNAMiRNAsMicroRNAsPathwayMicroRNPs
1998
Modifications of U2 snRNA are required for snRNP assembly and pre‐mRNA splicing
Yu Y, Shu M, Steitz J. Modifications of U2 snRNA are required for snRNP assembly and pre‐mRNA splicing. The EMBO Journal 1998, 17: 5783-5795. PMID: 9755178, PMCID: PMC1170906, DOI: 10.1093/emboj/17.19.5783.Peer-Reviewed Original ResearchConceptsEnd of U2Native gel analysisPre-mRNA splicingU2 snRNP particleGlycerol gradient analysisPseudouridylation activityGuanosine capSnRNP assemblySpliceosomal snRNAsSplicing activityTMG capSpliceosome assemblyU2 RNAU2 snRNAU2 functionProtein profilesGel analysisSnRNP particlesXenopus oocytesInternal modificationSnRNASplicingPotent inhibitorU2Extensive modification
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
1993
Rare scleroderma autoantibodies to the U11 small nuclear ribonucleoprotein and to the trimethylguanosine cap of U small nuclear RNAs.
Gilliam AC, Steitz JA. Rare scleroderma autoantibodies to the U11 small nuclear ribonucleoprotein and to the trimethylguanosine cap of U small nuclear RNAs. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 6781-6785. PMID: 8341699, PMCID: PMC47016, DOI: 10.1073/pnas.90.14.6781.Peer-Reviewed Original ResearchConceptsSmall nuclear ribonucleoprotein particleTrimethylguanosine capLow-abundance membersSmall nuclear RNASmall nuclear ribonucleoproteinNuclear ribonucleoprotein particleGlycerol gradient fractionsU RNAU11 small nuclear ribonucleoproteinsSnRNP complexTargeted degradationNuclear RNANuclear ribonucleoproteinRibonucleoprotein particleNuclear extractsSm classProtein componentsHeLa cellsRNPGradient fractionsRNAProteinScleroderma seraRibonucleoproteinCosediments