2021
STL-seq reveals pause-release and termination kinetics for promoter-proximal paused RNA polymerase II transcripts
Zimmer JT, Rosa-Mercado NA, Canzio D, Steitz JA, Simon MD. STL-seq reveals pause-release and termination kinetics for promoter-proximal paused RNA polymerase II transcripts. Molecular Cell 2021, 81: 4398-4412.e7. PMID: 34520723, PMCID: PMC9020433, DOI: 10.1016/j.molcel.2021.08.019.Peer-Reviewed Original ResearchConceptsPause releaseRNA polymerase II transcriptsRNA polymerase II moleculesCis-acting DNA elementsTATA box-containing promotersPolymerase II transcriptsPromoter-proximal pausingCritical regulatory functionsTranscriptional regulationRNA turnoverTranscriptional controlDNA elementsTranscriptional shutdownPause sitesHyperosmotic stressRegulatory mechanismsRegulatory functionsPrinciples of regulationHormonal stimuliPausingPremature terminationTranscriptsRegulation
2001
Proximity of the invariant loop of U5 snRNA to the second intron residue during pre‐mRNA splicing
McConnell T, Steitz J. Proximity of the invariant loop of U5 snRNA to the second intron residue during pre‐mRNA splicing. The EMBO Journal 2001, 20: 3577-3586. PMID: 11432844, PMCID: PMC125517, DOI: 10.1093/emboj/20.13.3577.Peer-Reviewed Original ResearchAnimalsAzidesBase SequenceCross-Linking ReagentsEnhancer Elements, GeneticGlobinsIntronsKineticsMammalsModels, MolecularMolecular Sequence DataNucleic Acid ConformationPlasmidsPolymerase Chain ReactionRibonuclease HRibonucleoproteins, Small NuclearRNA PrecursorsRNA SplicingRNA, Small NuclearThionucleotidesA novel embryonic poly(A) binding protein, ePAB, regulates mRNA deadenylation in Xenopus egg extracts
Voeltz GK, Ongkasuwan J, Standart N, Steitz JA. A novel embryonic poly(A) binding protein, ePAB, regulates mRNA deadenylation in Xenopus egg extracts. Genes & Development 2001, 15: 774-788. PMID: 11274061, PMCID: PMC312653, DOI: 10.1101/gad.872201.Peer-Reviewed Original ResearchAdenosine MonophosphateAmino Acid SequenceAnimalsBase SequenceBlotting, WesternDNA MethylationGene Expression Regulation, DevelopmentalKineticsMolecular Sequence DataOocytesPlasmidsPoly APoly(A)-Binding ProteinsPrecipitin TestsProtein BindingRecombinant ProteinsRNA-Binding ProteinsSequence Analysis, DNASequence Homology, Amino AcidTime FactorsTranscriptional ActivationUltraviolet RaysXenopusXenopus Proteins
1992
Site-specific cross-linking of mammalian U5 snRNP to the 5' splice site before the first step of pre-mRNA splicing.
Wyatt JR, Sontheimer EJ, Steitz JA. Site-specific cross-linking of mammalian U5 snRNP to the 5' splice site before the first step of pre-mRNA splicing. Genes & Development 1992, 6: 2542-2553. PMID: 1340469, DOI: 10.1101/gad.6.12b.2542.Peer-Reviewed Original ResearchConceptsSplice siteMRNA splicingATP-dependent interactionHeLa nuclear extractsU5 snRNPMRNA substratesSplice site regionProtein factorsU5 snRNANucleotides upstreamU6 snRNAPre-mRNANuclear extractsSplicingSite regionLoop sequenceCross-link formationSnRNASplicing conditionsWatson-Crick complementarityCross-linking strategyU1Selective photoactivationSnRNPMammalian
1989
Function of the mammalian La protein: evidence for its action in transcription termination by RNA polymerase III.
Gottlieb E, Steitz JA. Function of the mammalian La protein: evidence for its action in transcription termination by RNA polymerase III. The EMBO Journal 1989, 8: 851-861. PMID: 2470590, PMCID: PMC400884, DOI: 10.1002/j.1460-2075.1989.tb03446.x.Peer-Reviewed Original ResearchConceptsRNA polymerase III transcriptionPolymerase III transcriptionRNA polymerase IIITranscription complexPolymerase IIILa proteinTranscription termination factorFull-length transcriptsTranscription terminationTermination factorRNA productsTranscription intermediatesTranscriptsTranscriptionProteinComplexesPolymeraseRegulatorAbsence[31] Determination of RNA-protein and RNA-ribonucleoprotein interactions by nuclease probing
Parker K, Steitz J. [31] Determination of RNA-protein and RNA-ribonucleoprotein interactions by nuclease probing. Methods In Enzymology 1989, 180: 454-468. PMID: 2482428, DOI: 10.1016/0076-6879(89)80117-x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodiesCarrier ProteinsElectrophoresis, Polyacrylamide GelEndoribonucleasesHumansIndicators and ReagentsKineticsMiceMicrococcal NucleaseNucleotide MappingRibonuclease HRibonuclease T1RibonucleasesRibonucleoproteinsRNARNA PrecursorsRNA SplicingRNA-Binding ProteinsRNA, Ribosomal, 28STranscription, Genetic
1979
The 3′ terminus of 16S rRNA: secondary structure and interaction with ribosomal protein S1
Yuan R, Steitz J, Moore P, Crothers D. The 3′ terminus of 16S rRNA: secondary structure and interaction with ribosomal protein S1. Nucleic Acids Research 1979, 7: 2399-2418. PMID: 392471, PMCID: PMC342392, DOI: 10.1093/nar/7.8.2399.Peer-Reviewed Original Research