2024
Emerging and re-emerging themes in co-transcriptional pre-mRNA splicing
Carrocci T, Neugebauer K. Emerging and re-emerging themes in co-transcriptional pre-mRNA splicing. Molecular Cell 2024, 84: 3656-3666. PMID: 39366353, PMCID: PMC11463726, DOI: 10.1016/j.molcel.2024.08.036.Peer-Reviewed Original ResearchConceptsPre-mRNA splicingCo-transcriptional pre-mRNA splicingCo-transcriptional RNA foldingCo-transcriptional processesRNA polymerase IIPre-messenger RNAFunctional messenger RNAsCapping enzymePolymerase IIDelayed splicingPolyadenylation machinerySplicing eventsPre-mRNAGene regulationMacromolecular machinesRNA foldingRNA synthesisMRNA isoformsProtein productionGene expressionSplicingRNARegulatory importanceCross-regulationMessenger RNA
2016
Activation of transcription enforces the formation of distinct nuclear bodies in zebrafish embryos
Heyn P, Salmonowicz H, Rodenfels J, Neugebauer KM. Activation of transcription enforces the formation of distinct nuclear bodies in zebrafish embryos. RNA Biology 2016, 14: 752-760. PMID: 27858508, PMCID: PMC5519242, DOI: 10.1080/15476286.2016.1255397.Peer-Reviewed Original ResearchConceptsHistone locus bodyCajal bodiesNuclear bodiesSm ringHistone mRNA 3' end processingEnd processingMRNA 3' end processingDifferent nuclear bodiesDistinct nuclear bodiesNuclear body componentsDistinct regulatory functionsHLB formationHistone genesHistone transcriptsZygotic transcriptionTranscriptional silenceSplicing machineryRRNA processingEarly embryogenesisU7 snRNPNascent histoneZebrafish embryosDanio rerioCellular compartmentsTranscription inhibitionSplicing of Nascent RNA Coincides with Intron Exit from RNA Polymerase II
Oesterreich F, Herzel L, Straube K, Hujer K, Howard J, Neugebauer KM. Splicing of Nascent RNA Coincides with Intron Exit from RNA Polymerase II. Cell 2016, 165: 372-381. PMID: 27020755, PMCID: PMC4826323, DOI: 10.1016/j.cell.2016.02.045.Peer-Reviewed Original ResearchConceptsRNA polymerase IIPolymerase IIPol IIProtein-coding genesPol II progressionRNA sequencing methodsGene expression pathwaysRate of transcriptionEndogenous genesSplicing catalysisSplicing profilesSpliceosome assemblyExpression pathwaysSpliced productsGene expressionIntronsSplicingSequencing methodsMechanistic insightsGenesRegulationKinetic competitionEukaryotesSpliceosomeTranscription
2013
The nuclear cap-binding complex interacts with the U4/U6·U5 tri-snRNP and promotes spliceosome assembly in mammalian cells
Pabis M, Neufeld N, Steiner MC, Bojic T, Shav-Tal Y, Neugebauer KM. The nuclear cap-binding complex interacts with the U4/U6·U5 tri-snRNP and promotes spliceosome assembly in mammalian cells. RNA 2013, 19: 1054-1063. PMID: 23793891, PMCID: PMC3708526, DOI: 10.1261/rna.037069.112.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesGenes, fosGuanosineHeLa CellsHumansModels, BiologicalNuclear Cap-Binding Protein ComplexProtein Interaction Domains and MotifsRibonucleoprotein, U1 Small NuclearRibonucleoprotein, U4-U6 Small NuclearRibonucleoprotein, U5 Small NuclearRNA InterferenceRNA PrecursorsRNA SplicingSpliceosomesConceptsCap-binding complexCotranscriptional spliceosome assemblyU4/Spliceosome assemblySpliceosomal snRNPsRNA polymerase II transcriptsNuclear cap-binding complexPolymerase II transcriptsRecruitment of U1RNA-independent fashionActive transcription unitsPre-mRNA splicingLive-cell imaging assaysNonsense-mediated decayNetwork of interactionsRNA biogenesisGuanosine capSnRNP biogenesisMiRNA biogenesisTri-snRNPSnRNA exportSnRNP proteinsTranscription unitChromatin immunoprecipitationMammalian cells
2011
Cotranscriptional spliceosome assembly and splicing are independent of the Prp40p WW domain
Görnemann J, Barrandon C, Hujer K, Rutz B, Rigaut G, Kotovic KM, Faux C, Neugebauer KM, Séraphin B. Cotranscriptional spliceosome assembly and splicing are independent of the Prp40p WW domain. RNA 2011, 17: 2119-2129. PMID: 22020974, PMCID: PMC3222125, DOI: 10.1261/rna.02646811.Peer-Reviewed Original ResearchConceptsC-terminal domainWW domainsSpliceosome assemblyU1 snRNPPol II C-terminal domainCotranscriptional spliceosome assemblyComplex cellular functionsRNA polymerase IIProtein-protein interactionsPre-mRNA splicingU2 snRNP recruitmentSplice site recognitionCotranscriptional recruitmentTranscriptional machineryPolymerase IIPol IIU5 snRNPLarge subunitSplicing factorsCellular functionsStable heterodimerComplex assemblyPrp40Spliceosome formationAffinity purificationThe In Vivo Kinetics of RNA Polymerase II Elongation during Co-Transcriptional Splicing
Brody Y, Neufeld N, Bieberstein N, Causse SZ, Böhnlein EM, Neugebauer KM, Darzacq X, Shav-Tal Y. The In Vivo Kinetics of RNA Polymerase II Elongation during Co-Transcriptional Splicing. PLOS Biology 2011, 9: e1000573. PMID: 21264352, PMCID: PMC3019111, DOI: 10.1371/journal.pbio.1000573.Peer-Reviewed Original ResearchMeSH KeywordsBeta-GlobinsFluorescence Recovery After PhotobleachingGreen Fluorescent ProteinsHumansIntronsInverted Repeat SequencesLac RepressorsRecombinant Fusion ProteinsRibonucleoproteins, Small NuclearRNA Polymerase IIRNA PrecursorsRNA SplicingRNA, MessengerSpliceosomesTranscription, GeneticTumor Cells, CulturedConceptsNumber of intronsU1 snRNPPol II elongation ratesRNA polymerase II elongationRNA polymerase II enzymeSplicing-independent roleTranscription elongation kineticsIntron-containing genesCo-transcriptional splicingPolymerase II elongationCompletion of splicingTranscribed pre-mRNARNA processing eventsInducible gene constructsPol II elongationElongation ratePolymerase elongation ratesNascent RNATranscriptional elongationIntronless genesSpliceosome componentsTranscription terminationSplicing machineryTranscription sitesGene end
2010
The differential interaction of snRNPs with pre-mRNA reveals splicing kinetics in living cells
Huranová M, Ivani I, Benda A, Poser I, Brody Y, Hof M, Shav-Tal Y, Neugebauer KM, Staněk D. The differential interaction of snRNPs with pre-mRNA reveals splicing kinetics in living cells. Journal Of Cell Biology 2010, 191: 75-86. PMID: 20921136, PMCID: PMC2953428, DOI: 10.1083/jcb.201004030.Peer-Reviewed Original ResearchConceptsSmall nuclear RNP particlesPrecursor messenger RNA splicingMessenger RNA splicingBinding of U1Live-cell imagingRate of splicingNuclear RNP particlesLarge ribonucleoproteinSnRNP componentsRNA splicingSpliceosome assemblyAdditional proteinsRNP particlesHuman cellsSplicingLiving cellsCell nucleiDifferential interactionsEndogenous levelsSpliceosomeMRNARibonucleoproteinCell imagingCore componentCells
1995
A conserved epitope on a subset of SR proteins defines a larger family of Pre-mRNA splicing factors.
Neugebauer K, Stolk J, Roth M. A conserved epitope on a subset of SR proteins defines a larger family of Pre-mRNA splicing factors. Journal Of Cell Biology 1995, 129: 899-908. PMID: 7538140, PMCID: PMC2120486, DOI: 10.1083/jcb.129.4.899.Peer-Reviewed Original Research