2014
The Noncoding RNA Revolution—Trashing Old Rules to Forge New Ones
Cech TR, Steitz JA. The Noncoding RNA Revolution—Trashing Old Rules to Forge New Ones. Cell 2014, 157: 77-94. PMID: 24679528, DOI: 10.1016/j.cell.2014.03.008.Peer-Reviewed Original ResearchConceptsBiological functionsRNA-protein complexesLevel of transcriptionForeign nucleic acidsMost ncRNAsLong ncRNAsNcRNA researchRNA processingGenome rearrangementsNucleic acidsNoncoding RNAsGene expressionRNA structureNcRNAsBase pairingDNA synthesisRemarkable varietySnoRNPsRiboswitchGenomeSnRNPsRNAsRibosomesTranscriptionTelomerase
2002
The Divergent U12-Type Spliceosome Is Required for Pre-mRNA Splicing and Is Essential for Development in Drosophila
Otake LR, Scamborova P, Hashimoto C, Steitz JA. The Divergent U12-Type Spliceosome Is Required for Pre-mRNA Splicing and Is Essential for Development in Drosophila. Molecular Cell 2002, 9: 439-446. PMID: 11864616, DOI: 10.1016/s1097-2765(02)00441-0.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAnimalsAnimals, Genetically ModifiedBase SequenceDrosophila melanogasterDrosophila ProteinsGenes, LethalIntronsLarvaMolecular Sequence DataMutagenesis, InsertionalNerve Tissue ProteinsNuclear ProteinsNucleic Acid ConformationProtein IsoformsRibonucleoprotein, U4-U6 Small NuclearRibonucleoproteins, Small NuclearRNA PrecursorsRNA SplicingRNA, Small NuclearSequence AlignmentSequence Homology, Nucleic AcidSpliceosomesTranscription FactorsTransgenesConceptsU12-type spliceosomeThird instar larvalU12-type intronsPre-mRNA splicingU4atac/U6atacMetazoan organismsHomeodomain proteinsU5 snRNPsDrosophila melanogasterU12 spliceosomeMRNA intronsU12 snRNASingle locusU6atacInstar larvalSpliceosomeEmbryonic stagesCNS developmentIntronsMinor classU12DrosophilaMelanogasterVertebratesSnRNPs
1994
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 systemIntronsSnRNPsSequence and structural elements critical for U8 snRNP function in Xenopus oocytes are evolutionarily conserved.
Peculis BA, Steitz JA. Sequence and structural elements critical for U8 snRNP function in Xenopus oocytes are evolutionarily conserved. Genes & Development 1994, 8: 2241-2255. PMID: 7958892, DOI: 10.1101/gad.8.18.2241.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBiological EvolutionChromosomal Proteins, Non-HistoneConserved SequenceFemaleMethylationMolecular Sequence DataMutagenesis, Site-DirectedMutationNucleic Acid ConformationOocytesRibonucleoproteins, Small NuclearRNA CapsRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, Small NuclearXenopus
1991
An intact Box C sequence in the U3 snRNA is required for binding of fibrillarin, the protein common to the major family of nucleolar snRNPs.
Baserga SJ, Yang XD, Steitz JA. An intact Box C sequence in the U3 snRNA is required for binding of fibrillarin, the protein common to the major family of nucleolar snRNPs. The EMBO Journal 1991, 10: 2645-2651. PMID: 1714385, PMCID: PMC452965, DOI: 10.1002/j.1460-2075.1991.tb07807.x.Peer-Reviewed Original ResearchConceptsBox CU3 snRNANucleolar small RNAsSite-specific mutationsShort nucleotide sequencesFibrillarin proteinSmall RNAsDeletion analysisCommon binding siteBox DNucleotide sequenceSnRNPsMajor familiesSnRNAU3 snRNPRNAInput RNAFibrillarinBinding sitesC sequencesBindingProteinSequenceAnti-fibrillarin autoantibodiesBiogenesisMultiple 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
1990
Spliced leader RNA sequences can substitute for the essential 5′ end of U1 RNA during splicing in a mammalian in vitro system
Bruzik J, Steitz J. Spliced leader RNA sequences can substitute for the essential 5′ end of U1 RNA during splicing in a mammalian in vitro system. Cell 1990, 62: 889-899. PMID: 2168293, DOI: 10.1016/0092-8674(90)90264-f.Peer-Reviewed Original Research
1989
U3, U8 and U13 comprise a new class of mammalian snRNPs localized in the cell nucleolus.
Tyc K, Steitz JA. U3, U8 and U13 comprise a new class of mammalian snRNPs localized in the cell nucleolus. The EMBO Journal 1989, 8: 3113-3119. PMID: 2531075, PMCID: PMC401391, DOI: 10.1002/j.1460-2075.1989.tb08463.x.Peer-Reviewed Original Research
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
1985
Association of the lupus antigen La with a subset of U6 snRNA molecules
Rinke J, Steitz J. Association of the lupus antigen La with a subset of U6 snRNA molecules. Nucleic Acids Research 1985, 13: 2617-2629. PMID: 2582364, PMCID: PMC341179, DOI: 10.1093/nar/13.7.2617.Peer-Reviewed Original Research
1982
Small RNPs in eucaryotic cells
Hendrick J, Mount S, Rinke J, Wolin S, Rosa M, Gottlieb E, Lerner M, Steitz J. Small RNPs in eucaryotic cells. 1982, 321-328. DOI: 10.1007/978-1-349-06343-7_44.Peer-Reviewed Original ResearchSmall nuclear RNAAbundant small nuclear RNAsRNA-protein complexesEukaryotic cellsSmall RNAsSmall ribonucleoproteinSubcellular locationNuclear RNARNA componentU1 snRNPsEucaryotic cellsComponent RNARibonucleoproteinRNP particlesRNAInitial discoveryProteinPartial characterizationState of maturationSnRNPsCellsSystemic lupus erythematosusDiversityMaturationMetabolism
1980
Are snRNPs involved in splicing?
Lerner M, Boyle J, Mount S, Wolin S, Steitz J. Are snRNPs involved in splicing? Nature 1980, 283: 220-224. PMID: 7350545, DOI: 10.1038/283220a0.Peer-Reviewed Original ResearchConceptsSmall nuclear RNA speciesProminent nuclear proteinsRNA-protein complexesSmall RNA moleculesSmall nuclear ribonucleoproteinNuclear RNA speciesSnRNA speciesSnRNAs U1RNA speciesU6 RNASnRNA moleculesNuclear proteinsNuclear ribonucleoproteinNucleotide sequenceU1 RNARNA moleculesSnRNPsExtensive complementaritySplice junctionsNuclear locationLines of evidenceAnti-Sm seraCell nucleiHnRNA moleculesMouse Ehrlich