2023
Nucleolar structure connects with global nuclear organization.
Wang C, Ma H, Baserga S, Pederson T, Huang S. Nucleolar structure connects with global nuclear organization. Molecular Biology Of The Cell 2023, 34: ar114. PMID: 37610836, PMCID: PMC10846622, DOI: 10.1091/mbc.e23-02-0062.Peer-Reviewed Original ResearchConceptsNucleolar structureGenomic lociNuclear domainsSpecific genomic lociGlobal nuclear organizationRNA processing factorsRNA polymerase ICajal bodiesNuclear organizationRibosome synthesisNuclear bodiesKnockdown cellsPerinucleolar compartmentPolymerase IIntranuclear locationHeLa cellsNucleolar segregationSpatial organizationNucleoliLociUtp4CellsRPA194SegregationCompositional changesHuman 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
2016
Probing the mechanisms underlying human diseases in making ribosomes.
Farley KI, Baserga SJ. Probing the mechanisms underlying human diseases in making ribosomes. Biochemical Society Transactions 2016, 44: 1035-44. PMID: 27528749, PMCID: PMC5360156, DOI: 10.1042/bst20160064.Peer-Reviewed Original ResearchThe Contributions of the Ribosome Biogenesis Protein Utp5/WDR43 to Craniofacial Development
Sondalle SB, Baserga SJ, Yelick PC. The Contributions of the Ribosome Biogenesis Protein Utp5/WDR43 to Craniofacial Development. Journal Of Dental Research 2016, 95: 1214-1220. PMID: 27221611, PMCID: PMC5076753, DOI: 10.1177/0022034516651077.Peer-Reviewed Original ResearchConceptsRibosomal proteinsCraniofacial developmentRibosome biogenesis proteinsRibosomal protein functionHuman craniofacial developmentTissue-specific defectsDiverse cell typesHuman ribosomopathiesBiogenesis proteinsTranslational machineryProtein functionDistinct functionsTranslational mechanismsTissue differentiationCell typesWDR43Global defectsProteinExciting researchSurprising similaritiesUnderstanding of rolesRibosomopathiesBiogenesisMachineryMutationsThe 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 systemYeastFoldingProteinNOP4
2001
Fibrillarin and Other snoRNP Proteins Are Targets of Autoantibodies in Xenobiotic-Induced Autoimmunity
Yang J, Baserga S, Turley S, Pollard K. Fibrillarin and Other snoRNP Proteins Are Targets of Autoantibodies in Xenobiotic-Induced Autoimmunity. Clinical Immunology 2001, 101: 38-50. PMID: 11580225, DOI: 10.1006/clim.2001.5099.Peer-Reviewed Original ResearchConceptsSJL/J miceSmall nucleolar ribonucleoproteinSnoRNP proteinsCajal bodiesNucleolar ribonucleoproteinMetaphase chromosomesAmphibian cellsJ miceFibrillarinInterphase cellsProtein componentsNucleolar immunofluorescence patternProteinAnti-nucleolar antibodiesCell linesTarget of autoantibodiesAutoantibody responseAntibody responsePredominant targetImmunofluorescence patternMurineCellsRibonucleoproteinChromosomesMice
1999
Human Nop5/Nop58 is a component common to the box C/D small nucleolar ribonucleoproteins.
Lyman S, Gerace L, Baserga S. Human Nop5/Nop58 is a component common to the box C/D small nucleolar ribonucleoproteins. RNA 1999, 5: 1597-604. PMID: 10606270, PMCID: PMC1369881, DOI: 10.1017/s1355838299991288.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsCell NucleolusCloning, MolecularConserved SequenceHeLa CellsHumansMiceMolecular Sequence DataMolecular WeightNuclear ProteinsRatsRecombinant ProteinsRibonucleoproteinsRibonucleoproteins, Small NucleolarSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino Acid
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
1997
Mpp10p, a U3 Small Nucleolar Ribonucleoprotein Component Required for Pre-18S rRNA Processing in Yeast
Dunbar D, Wormsley S, Agentis T, Baserga S. Mpp10p, a U3 Small Nucleolar Ribonucleoprotein Component Required for Pre-18S rRNA Processing in Yeast. Molecular And Cellular Biology 1997, 17: 5803-5812. PMID: 9315638, PMCID: PMC232428, DOI: 10.1128/mcb.17.10.5803.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodiesCloning, MolecularEscherichia coliGenes, FungalHumansMiceMolecular Sequence DataMolecular WeightPhosphoproteinsRecombinant Fusion ProteinsRibonucleoproteinsRibonucleoproteins, Small NuclearRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, RibosomalRNA, Ribosomal, 18SSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSpores, FungalConceptsYeast proteinsU3 snoRNPProtein componentsU3 small nucleolar ribonucleoproteinNovel protein componentsPre-rRNA processingSmall nucleolar ribonucleoproteinS. cerevisiae cellsSpecific protein componentsPulse-chase analysisMitotic phosphorylationRibosome biogenesisEssential genesMpp10pYeast SaccharomycesNovel proteinU3 snoRNARRNA precursorNucleolar ribonucleoproteinSites A0Tetrad analysisHuman proteinsNull allelesCerevisiae cellsGenBank searchMpp10p, a new protein component of the U3 snoRNP required for processing of 18S rRNA precursors.
Baserga S, Agentis T, Wormsley S, Dunbar D, Lee S. Mpp10p, a new protein component of the U3 snoRNP required for processing of 18S rRNA precursors. Nucleic Acids Symposium Series 1997, 64-7. PMID: 9478208.Peer-Reviewed Original ResearchConceptsPre-rRNA processingNew protein componentsU3 snoRNPProtein componentsU3 small nucleolar ribonucleoproteinSmall nucleolar ribonucleoproteinEssential genesSlow growthConditional promoterU3 snoRNAMpp10pNucleolar ribonucleoproteinRRNA precursorProcessing eventsYeastSnoRNPsMpp10ProteinModel systemDegrees C. AnalysisC. AnalysisSnoRNAsMutantsRibonucleoproteinSaccharomyces
1992
Beta-globin nonsense mutation: deficient accumulation of mRNA occurs despite normal cytoplasmic stability.
Baserga S, Benz E. Beta-globin nonsense mutation: deficient accumulation of mRNA occurs despite normal cytoplasmic stability. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 2935-2939. PMID: 1557399, PMCID: PMC48778, DOI: 10.1073/pnas.89.7.2935.Peer-Reviewed Original ResearchConceptsMRNA metabolismHeterologous transfection systemRNA polymerase IIHuman beta-globin geneMetabolism of mRNAAmber nonsense mutationsAnalysis of transcriptionAccumulation of mRNARNA expression studiesBeta-globin genePolymerase IIMRNA polyadenylationCytoplasmic stabilityMRNA stabilityExpression studiesPermanent cell linesProtein synthesisTransfection systemMediterranean populationsNonsense mutationSplicing accuracyMutationsDeficient accumulationCell linesMRNA
1991
Three pseudogenes for human U13 snRNA belong to class III
Baserga S, Yang X, Steitz J. Three pseudogenes for human U13 snRNA belong to class III. Gene 1991, 107: 347-348. PMID: 1748306, DOI: 10.1016/0378-1119(91)90340-h.Peer-Reviewed Original Research
1990
Metabolism of Non‐Translatable Globin mRNAs Arising from Premature Translation Termination Codons
MAGNUS T, BASERGA S, STOLLE C, TAKESHITA K, BENZ E. Metabolism of Non‐Translatable Globin mRNAs Arising from Premature Translation Termination Codons. Annals Of The New York Academy Of Sciences 1990, 612: 55-66. PMID: 2291574, DOI: 10.1111/j.1749-6632.1990.tb24290.x.Peer-Reviewed Original Research
1988
Nonsense mutations in the human beta-globin gene affect mRNA metabolism.
Baserga S, Benz E. Nonsense mutations in the human beta-globin gene affect mRNA metabolism. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 2056-2060. PMID: 3353367, PMCID: PMC279927, DOI: 10.1073/pnas.85.7.2056.Peer-Reviewed Original ResearchConceptsHeterologous transfection systemBeta-globin mRNABeta-globin geneNonsense mutationHuman beta-globin geneTransfection systemTranslation termination codonPeripheral blood cellsHuman beta-globin mRNATranslation termination mutationsMammalian mRNAsMRNA metabolismBeta 17Steady-state levelsTermination codonMRNA accumulationNormal levelsTypes of mutationsTermination mutationsBlood cellsMissense mutationsGenesHuman alphaMutationsZero-thalassemia
1985
Polyadenylation of a human mitochondrial ribosomal RNA transcript detected by molecular cloning
Baserga S, Linnenbach A, Malcolm S, Ghosh P, Malcolm A, Takeshita K, Forget B, Benz E. Polyadenylation of a human mitochondrial ribosomal RNA transcript detected by molecular cloning. Gene 1985, 35: 305-312. PMID: 4043734, DOI: 10.1016/0378-1119(85)90009-5.Peer-Reviewed Original Research