2018
High throughput discovery of novel regulators of human ribosome biogenesis
Baserga S, Farley‐Barnes K, McCann K, Ogawa L, Merkel J, Surovtseva Y. High throughput discovery of novel regulators of human ribosome biogenesis. The FASEB Journal 2018, 32: 526.25-526.25. DOI: 10.1096/fasebj.2018.32.1_supplement.526.25.Peer-Reviewed Original ResearchRibosome biogenesisNucleolar functionNumber of nucleoliMammalian cellsGenome-wide siRNA screenRNA polymerase I transcriptionHuman ribosome biogenesisPre-ribosomal RNAPolymerase I transcriptionExperimental Biology 2018 MeetingHigh-throughput discoveryNucleolar proteinsRibosomal DNAProtein regulatorsI transcriptionNew regulatorNovel regulatorSiRNA screenBiogenesisHuman cellsProteinRegulatorNucleoliFASEB JournalThroughput discovery
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 systemYeastFoldingProteinNOP4Discovery of mammalian regulators of ribosome biogenesis
Farley K, McCann K, Merkel J, Surovtseva Y, Baserga S. Discovery of mammalian regulators of ribosome biogenesis. The FASEB Journal 2016, 30 DOI: 10.1096/fasebj.30.1_supplement.594.1.Peer-Reviewed Original ResearchRibosome biogenesisNucleolar functionNumber of nucleoliGenome-wide siRNA screenRNA polymerase I transcriptionPre-ribosomal RNAPolymerase I transcriptionMammalian regulatorsChromatin stateNucleolar proteinsRibosomal DNAMammalian cellsProtein regulatorsI transcriptionNew regulatorSiRNA screenBiogenesisNucleolar numberHuman cellsProteinRegulatorNucleoliNew roleCellsNew pathwayWhen 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
2014
Discovering the pre‐60S ribosome biogenesis factor interactome (560.7)
McCann K, Charette J, Vincent N, Baserga S. Discovering the pre‐60S ribosome biogenesis factor interactome (560.7). The FASEB Journal 2014, 28 DOI: 10.1096/fasebj.28.1_supplement.560.7.Peer-Reviewed Original ResearchRibosome assemblyGlycerol gradient sedimentation analysisTwo-hybrid analysisHigh-throughput yeastHigh-confidence interactionsPotential regulatory mechanismsGradient sedimentation analysisRNA helicasesBiogenesis factorsSmaller subcomplexesMDa complexNucleolar proteinsRibosomal subunitRegulatory mechanismsDifferent proteinsSubcomplexHelicasesGlycerol gradientsIndependent validation experimentsInteractomeSedimentation analysisYeastCurrent knowledgeProteinAssembly
2013
NOL11, implicated in the pathogenesis of North American Indian Childhood Cirrhosis, is required for pre‐rRNA transcription and processing
Baserga S, Freed E, Prieto J, McCann K, McStay B. NOL11, implicated in the pathogenesis of North American Indian Childhood Cirrhosis, is required for pre‐rRNA transcription and processing. The FASEB Journal 2013, 27: 552.1-552.1. DOI: 10.1096/fasebj.27.1_supplement.552.1.Peer-Reviewed Original ResearchNorth American Indian childhood cirrhosisRibosome biogenesisSmall subunitC-terminusInteraction partnersDefective protein-protein interactionsTwo-hybrid cDNA libraryUncharacterized nucleolar proteinRibosome biogenesis factorsRibosome biogenesis defectsTwo-hybrid analysisPre-rRNA transcriptionRibosomal small subunitProtein-protein interactionsCo-immunoprecipitation experimentsRDNA transcriptionBiogenesis defectsBiogenesis factorsNucleolar proteinsNovel proteinCDNA libraryCirhinAffinity purificationDisease mutationsSiRNA knockdown
2000
A nucleolar protein related to ribosomal protein L7 is required for an early step in large ribosomal subunit biogenesis
Dunbar D, Dragon F, Lee S, Baserga S. A nucleolar protein related to ribosomal protein L7 is required for an early step in large ribosomal subunit biogenesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 13027-13032. PMID: 11087857, PMCID: PMC27172, DOI: 10.1073/pnas.97.24.13027.Peer-Reviewed Original ResearchConceptsNucleolar proteinsLarge ribosomal subunit biogenesisLarge ribosomal subunit RNARibosomal subunit biogenesisRNA-binding domainRibosomal subunit RNAPulse-chase labeling experimentsProcessing of precursorsRibosomal protein L7Subunit biogenesisExonucleolytic trimmingEssential genesRibosomal proteinsSpecificity factorMature rRNAPrecursor RNASpacer 2L7 proteinSubunit RNAEndonucleolytic cleavageProtein L7Extensive identityRRNAMajor substratePrimer extension
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