2023
Human nucleolar protein 7 (NOL7) is required for early pre-rRNA accumulation and pre-18S rRNA processing
McCool M, Bryant C, Huang H, Ogawa L, Farley-Barnes K, Sondalle S, Abriola L, Surovtseva Y, Baserga S. Human nucleolar protein 7 (NOL7) is required for early pre-rRNA accumulation and pre-18S rRNA processing. RNA Biology 2023, 20: 257-271. PMID: 37246770, PMCID: PMC10228412, DOI: 10.1080/15476286.2023.2217392.Peer-Reviewed Original ResearchConceptsPre-rRNA accumulationRibosome biogenesisNonessential roleEukaryotic ribosome biogenesisEssential cellular processesNucleolar stress responsePre-rRNA levelsRRNA processingLikely orthologCellular processesAssociated proteinsTumor suppressorStress responseHuman cellsProtein synthesisProtein 7Human counterpartBiogenesisYeastOrthologsHomologSubcomplexAccumulationRRNATranscription
2022
Human pre-60S assembly factors link rRNA transcription to pre-rRNA processing
McCool M, Buhagiar A, Bryant C, Ogawa L, Abriola L, Surovtseva Y, Baserga S. Human pre-60S assembly factors link rRNA transcription to pre-rRNA processing. RNA 2022, 29: rna.079149.122. PMID: 36323459, PMCID: PMC9808572, DOI: 10.1261/rna.079149.122.Peer-Reviewed Original ResearchRRNA transcriptionRRNA processingRibosomal subunit biogenesisRNA polymerase IRibosome biosynthesisSubunit biogenesisRibosome biogenesisRibosome assemblyAssembly factorsTranscription controlBiogenesis factorsRRNA productionSteady-state levelsRNA transcriptionPolymerase IComplex membersHuman cellsProtein synthesisP53 stabilizationTranscriptionEssential processBiogenesisCell proliferationDual roleRegulatory details
2016
The molecular basis for ANE syndrome revealed by the large ribosomal subunit processome interactome
McCann KL, Teramoto T, Zhang J, Hall T, Baserga SJ. The molecular basis for ANE syndrome revealed by the large ribosomal subunit processome interactome. ELife 2016, 5: e16381. PMID: 27077951, PMCID: PMC4859800, DOI: 10.7554/elife.16381.Peer-Reviewed Original ResearchMeSH KeywordsAlopeciaCircular DichroismEndocrine System DiseasesHumansIntellectual DisabilityMagnetic Resonance SpectroscopyModels, BiologicalMutant ProteinsProtein BindingProtein FoldingProtein Interaction MapsRibonucleoproteins, Small NucleolarRibosome Subunits, LargeRNA PrecursorsRNA Processing, Post-TranscriptionalRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsProtein-protein interactionsANE syndromeMolecular basisDefective protein foldingRRNA processing defectsRNA recognition motifMature ribosomesRibosome assemblyHub proteinsRRNA processingNucleolar proteinsDomain foldingProtein foldingRecognition motifHuman diseasesProcessing defectsInteractomeMutationsCircular dichroismHub functionModel systemYeastFoldingProteinNOP4When Good Ribosomes Go Bad
Baserga S, McCann K, Teramoto T, Zhang J, Tanaka Hall T. When Good Ribosomes Go Bad. The FASEB Journal 2016, 30 DOI: 10.1096/fasebj.30.1_supplement.387.1.Peer-Reviewed Original ResearchProtein-protein interactionsRNA recognition motifANE syndromeRibosome biogenesisRRNA processingProtein functionMolecular basisPre-rRNA processing defectThird RNA recognition motifDefective protein foldingHuman genetic diseasesFull-length proteinSingle amino acid substitutionNumerous human disordersAmino acid substitutionsYeast orthologMature ribosomesEukaryotic cellsGood ribosomeRibosome synthesisHub proteinsNucleolar proteinsNucleolar functionDomain foldingNucleolar dysfunction
1999
Imp3p and Imp4p, Two Specific Components of the U3 Small Nucleolar Ribonucleoprotein That Are Essential for Pre-18S rRNA Processing
Lee S, Baserga S. Imp3p and Imp4p, Two Specific Components of the U3 Small Nucleolar Ribonucleoprotein That Are Essential for Pre-18S rRNA Processing. Molecular And Cellular Biology 1999, 19: 5441-5452. PMID: 10409734, PMCID: PMC84386, DOI: 10.1128/mcb.19.8.5441.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceGenes, ReporterGenetic TechniquesGenetic VectorsMacromolecular SubstancesMolecular Sequence DataPhosphoproteinsRecombinant Fusion ProteinsRibonucleoproteinsRibonucleoproteins, Small NuclearRibosomal ProteinsRNA PrecursorsRNA, FungalRNA, Ribosomal, 18SSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino AcidConceptsU3 small nucleolar ribonucleoproteinSmall nucleolar ribonucleoproteinProtein componentsU3 snoRNPNucleolar ribonucleoproteinGenetic depletionTwo-hybrid methodologyNovel protein componentsPre-rRNA processingUnique protein componentRibosomal proteinsSnoRNA levelsRRNA processingU3 snoRNARRNA precursorIMP proteinU3 RNAS4 familiesPrecise functionSevere defectsCleavage eventsMpp10pProteinSnoRNPsRNA
1998
M Phase Phosphoprotein 10 Is a Human U3 Small Nucleolar Ribonucleoprotein Component
Westendorf J, Konstantinov K, Wormsley S, Shu M, Matsumoto-Taniura N, Pirollet F, Klier F, Gerace L, Baserga S. M Phase Phosphoprotein 10 Is a Human U3 Small Nucleolar Ribonucleoprotein Component. Molecular Biology Of The Cell 1998, 9: 437-449. PMID: 9450966, PMCID: PMC25272, DOI: 10.1091/mbc.9.2.437.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCell FractionationCell NucleolusChromosomal Proteins, Non-HistoneCloning, MolecularDactinomycinDNA, ComplementaryHeLa CellsHumansIsoelectric PointMitosisMolecular Sequence DataMolecular WeightNuclear ProteinsPhosphoproteinsRibonucleoproteinsRibonucleoproteins, Small NuclearRNA, Small NuclearSequence Analysis, DNASpecies SpecificityConceptsM-phase phosphoproteinsPrenucleolar bodiesBox C/D snoRNAsU3 small nucleolar RNASmall nucleolar RNAsIsolation of cDNAsHuman U3D snoRNAsRRNA processingNucleolar proteinsP80-coilinNovel proteinNucleolar functionU3 snoRNAChromosome surfaceNucleolar RNAsCell fractionationMpp10FibrillarinInterphase cellsCell cycleRibonucleoprotein componentsM phaseProteinSnoRNAs
1996
The U18 snRNA is not essential for pre-rRNA processing in Xenopus laevis.
Dunbar D, Ware V, Baserga S. The U18 snRNA is not essential for pre-rRNA processing in Xenopus laevis. RNA 1996, 2: 324-33. PMID: 8634913, PMCID: PMC1369375.Peer-Reviewed Original Research