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
2012
First Exon Length Controls Active Chromatin Signatures and Transcription
Bieberstein NI, Oesterreich F, Straube K, Neugebauer KM. First Exon Length Controls Active Chromatin Signatures and Transcription. Cell Reports 2012, 2: 62-68. PMID: 22840397, DOI: 10.1016/j.celrep.2012.05.019.Peer-Reviewed Original ResearchConceptsGeneral transcription factorsTranscription start siteFirst exonShort first exonExon-intron organizationGenome-wide analysisHistone modifications H3K4me3Active chromatin signatureRNA polymerase IIRole of splicingTransgenic cell linesChIP-seq dataLong first exonChromatin signaturesGene architectureExon-intron boundariesHigh expression levelsAntisense transcriptionTranscriptional outputPolymerase IIH3K4me3 levelsGene activityTSS usageTranscription factorsExon lengthThe RNA-binding landscapes of two SR proteins reveal unique functions and binding to diverse RNA classes
Änkö ML, Müller-McNicoll M, Brandl H, Curk T, Gorup C, Henry I, Ule J, Neugebauer KM. The RNA-binding landscapes of two SR proteins reveal unique functions and binding to diverse RNA classes. Genome Biology 2012, 13: r17. PMID: 22436691, PMCID: PMC3439968, DOI: 10.1186/gb-2012-13-3-r17.Peer-Reviewed Original ResearchConceptsSR proteinsSR protein family membersHistone mRNA metabolismConsensus binding motifsProtein family membersIntron-containing mRNAsCellular regulatory mechanismsNonsense-mediated decayNon-coding RNAsNumerous RNAsHistone transcriptsMRNA metabolismUnique RNASplicing eventsAlternative splicingRNA classesRNA recognitionRelated RNATarget genesSRSF4Binding motifRegulatory mechanismsRNA targetsSRSF3Murine cells
2011
Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins
Tripsianes K, Madl T, Machyna M, Fessas D, Englbrecht C, Fischer U, Neugebauer KM, Sattler M. Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins. Nature Structural & Molecular Biology 2011, 18: 1414-1420. PMID: 22101937, DOI: 10.1038/nsmb.2185.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceArginineBinding SitesHumansModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiaryRibonucleoproteins, Small NuclearRNA Splicing FactorsSequence AlignmentSMN Complex ProteinsSurvival of Motor Neuron 1 ProteinThermodynamics
1997
Transcription units as RNA processing units
Neugebauer K, Roth M. Transcription units as RNA processing units. Genes & Development 1997, 11: 3279-3285. PMID: 9407022, DOI: 10.1101/gad.11.24.3279.Peer-Reviewed Original ResearchDistribution of pre-mRNA splicing factors at sites of RNA polymerase II transcription.
Neugebauer K, Roth M. Distribution of pre-mRNA splicing factors at sites of RNA polymerase II transcription. Genes & Development 1997, 11: 1148-1159. PMID: 9159396, DOI: 10.1101/gad.11.9.1148.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, MonoclonalBinding SitesCell NucleusFluorescent Antibody Technique, IndirectHeLa CellsHumansNuclear ProteinsPhosphoproteinsRibonucleoproteins, Small NuclearRNA Polymerase IIRNA PrecursorsRNA SplicingRNA-Binding ProteinsSerine-Arginine Splicing FactorsTranscription, GeneticUridine TriphosphateConceptsRNA polymerase II transcriptionPolymerase II transcriptionMRNA splicing factorsSplicing factorsSR familyPre-mRNA splicingVisualization of hundredsHeLa cell nucleiSplicing regulatorsActive genesTranscription unitMRNA splicingGene regulatorsGene transcriptionPre-mRNADistinct functionsRNA synthesisTranscriptionCell nucleiSplicingSingle memberRegulatorActive site