2024
A scalable and cost-efficient rRNA depletion approach to enrich RNAs for molecular biology investigations
Singh A, Xue A, Tai J, Mbadugha F, Obi P, Mascarenhas R, Tyagi A, Siena A, Chen Y. A scalable and cost-efficient rRNA depletion approach to enrich RNAs for molecular biology investigations. RNA 2024, 30: rna.079761.123. PMID: 38485192, PMCID: PMC11098455, DOI: 10.1261/rna.079761.123.Peer-Reviewed Original ResearchConceptsDepleting rRNACellular processesAbundance of rRNAMolecular biological investigationsNon-rRNA transcriptsComplex regulatory networkInvestigate gene expressionRRNA removalRRNA moleculesHistone mRNARegulatory networksSmall RNAsPositive selectionRRNARNA inputBiological investigationsTranscriptome analysisLong noncoding RNAsGene expressionRegulatory mechanismsRNAOff-target effectsNoncoding RNAsCircular RNAsTranscription
2016
The time-resolved transcriptome of C. elegans
Boeck ME, Huynh C, Gevirtzman L, Thompson OA, Wang G, Kasper DM, Reinke V, Hillier LW, Waterston RH. The time-resolved transcriptome of C. elegans. Genome Research 2016, 26: 1441-1450. PMID: 27531719, PMCID: PMC5052054, DOI: 10.1101/gr.202663.115.Peer-Reviewed Original ResearchConceptsTime-resolved transcriptomeAlternative splice formsPost-embryonic stagesRNA-seq dataLife cycleC. elegansNematode CaenorhabditisHistone mRNATranscriptional programsLate embryogenesisRNA-seqSplice formsPromoter usageSplice junctionsDifferential usageDetailed annotationGenesExpression correlatesCaenorhabditisElegansTranscriptomeOperonWormBaseEmbryogenesisSL1
2014
Nuclear bodies: RNA‐rich powerhouses of the cell (471.3)
Neugebauer K, Machyna M, Straube K, Heyn P. Nuclear bodies: RNA‐rich powerhouses of the cell (471.3). The FASEB Journal 2014, 28 DOI: 10.1096/fasebj.28.1_supplement.471.3.Peer-Reviewed Original ResearchHistone locus bodyCajal bodiesNuclear bodiesZygotic genome activationTrafficking of RNAsEarly zebrafish embryogenesisSites of transcriptionSite of assemblyGenome activationSpliceosomal snRNPsZebrafish embryogenesisRNA processingHistone mRNAMRNA splicingEnd formationMacromolecular complexesLow-affinity interactionsNuclear morphologyCell nucleiCommon organizational featuresLipid bilayersRNAEfficient assemblyDifferent functionsMolecular composition
2012
The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination
Krishnan N, Lam TT, Fritz A, Rempinski D, O'Loughlin K, Minderman H, Berezney R, Marzluff WF, Thapar R. The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination. Molecular And Cellular Biology 2012, 32: 4306-4322. PMID: 22907757, PMCID: PMC3486140, DOI: 10.1128/mcb.00382-12.Peer-Reviewed Original ResearchMeSH KeywordsCell CycleCell Line, TumorCell NucleusDown-RegulationHEK293 CellsHeLa CellsHistonesHumansmRNA Cleavage and Polyadenylation FactorsNIMA-Interacting Peptidylprolyl IsomeraseNuclear ProteinsPeptidylprolyl IsomeraseProtein Phosphatase 2RNA InterferenceRNA StabilityRNA-Binding ProteinsRNA, MessengerRNA, Small InterferingUbiquitinationConceptsStem-loop binding proteinHistone mRNADegradation of SLBPMRNA stabilityBinding proteinHistone mRNA stabilityRNA degradation machineryHistone mRNA decayS phaseProtein phosphatase 2AHistone mRNA degradationCore histone mRNAsExosome-mediated degradationDownregulation of Pin1Ubiquitin-proteasome systemMRNA 3' endsProlyl isomerase Pin1Phosphatase 2ADegradation machineryMRNA decayMRNA degradationProteasome systemIsomerase Pin1MRNA complexesUntranslated regionCajal bodies: where form meets function
Machyna M, Heyn P, Neugebauer KM. Cajal bodies: where form meets function. Wiley Interdisciplinary Reviews - RNA 2012, 4: 17-34. PMID: 23042601, DOI: 10.1002/wrna.1139.Peer-Reviewed Original ResearchConceptsCajal bodiesCB assemblyHistone locus bodyHistone gene clusterRibosome biogenesisGene clusterHistone mRNATelomere maintenanceCellular functionsRNA speciesWidespread mechanismCell nucleiSurprising complexityBiochemical processesAltered affinityBody assemblyAssembly propertiesRibonucleoproteinDistinct structuresAssemblyPre-existing substructuresBiogenesisSplicingAdditional layerTranscriptionInteraction of the Histone mRNA Hairpin with Stem–Loop Binding Protein (SLBP) and Regulation of the SLBP–RNA Complex by Phosphorylation and Proline Isomerization
Zhang M, Lam TT, Tonelli M, Marzluff WF, Thapar R. Interaction of the Histone mRNA Hairpin with Stem–Loop Binding Protein (SLBP) and Regulation of the SLBP–RNA Complex by Phosphorylation and Proline Isomerization. Biochemistry 2012, 51: 3215-3231. PMID: 22439849, PMCID: PMC3328597, DOI: 10.1021/bi2018255.Peer-Reviewed Original ResearchConceptsStem-loop binding proteinStem-loop structureHistone mRNAProline isomerizationThreonine phosphorylationEnd formationC base pairsReplication-dependent histone mRNAsBase pairsBinding proteinPossible structural roleAdjacent prolineHistone proteinsRibonucleoprotein complexesHelix motifMRNA hairpinsMRNA complexesUntranslated regionStructural roleFirst binding sitePhosphorylationProteinComplex dissociationCritical hingeMRNA
2008
Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′‐end maturation
Kolev NG, Yario TA, Benson E, Steitz JA. Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′‐end maturation. EMBO Reports 2008, 9: 1013-1018. PMID: 18688255, PMCID: PMC2572124, DOI: 10.1038/embor.2008.146.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceBase SequenceCell LineCleavage And Polyadenylation Specificity FactorConserved SequenceEndonucleasesEnzyme ActivationHeLa CellsHistonesHumansMolecular Sequence DataProtein Structure, TertiaryProtein SubunitsRNA 3' End ProcessingRNA PrecursorsRNA, MessengerConceptsPre-messenger RNAPolyadenylation specificity factorMammalian proteinsRNase ZConserved motifsHistone mRNASpecificity factorEndonucleolytic cleavageActive endonucleaseEndonuclease activityMBL familyComplex machineryMessenger RNAPoint mutationsCPSF73CPSF100Process of maturationMaturation processRNAProteinMotifMRNAMaturationEukaryotesCleavage
2005
Symplekin and multiple other polyadenylation factors participate in 3′-end maturation of histone mRNAs
Kolev NG, Steitz JA. Symplekin and multiple other polyadenylation factors participate in 3′-end maturation of histone mRNAs. Genes & Development 2005, 19: 2583-2592. PMID: 16230528, PMCID: PMC1276732, DOI: 10.1101/gad.1371105.Peer-Reviewed Original ResearchConceptsTail elongationU7 small nuclear ribonucleoproteinCommon molecular machineryMammalian cell extractsCleavage stimulation factorPolyadenylation specificity factorSmall nuclear ribonucleoproteinMolecular machineryHistone mRNAProtein complexesMRNA cleavageSpecificity factorPolyadenylation factorsTranslational activationNuclear ribonucleoproteinSymplekinReconstitution experimentsCell extractsHeat-labile factorMessenger RNAHistonesMRNAStimulation factorSubunitsCytoplasmic
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