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 ResearchMeSH KeywordsHumansNuclear ProteinsRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, Ribosomal, 18SRNA, Small NucleolarSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsPre-rRNA accumulationRibosome biogenesisNonessential roleEukaryotic ribosome biogenesisEssential cellular processesNucleolar stress responsePre-rRNA levelsRRNA processingLikely orthologCellular processesAssociated proteinsTumor suppressorStress responseHuman cellsProtein synthesisProtein 7Human counterpartBiogenesisYeastOrthologsHomologSubcomplexAccumulationRRNATranscription
2016
Nop9 is a PUF-like protein that prevents premature cleavage to correctly process pre-18S rRNA
Zhang J, McCann KL, Qiu C, Gonzalez LE, Baserga SJ, Hall TM. Nop9 is a PUF-like protein that prevents premature cleavage to correctly process pre-18S rRNA. Nature Communications 2016, 7: 13085. PMID: 27725644, PMCID: PMC5062617, DOI: 10.1038/ncomms13085.Peer-Reviewed Original ResearchConceptsEukaryotic ribosome biogenesisCorrect subcellular locationRibosome assembly factorsPre-ribosomal RNAPumilio repeatsRibosome biogenesisHuman ribosomopathiesAssembly factorsBiogenesis factorsRepeat proteinsMature rRNASubcellular locationNop9RNA complexCleavage siteRRNATimely cleavageProteinStructural featuresFinal processing stepRibosomopathiesBiogenesisCleavageYeastNucleaseThe 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
1998
The U14 snoRNA is required for 2'-O-methylation of the pre-18S rRNA in Xenopus oocytes.
Dunbar D, Baserga S. The U14 snoRNA is required for 2'-O-methylation of the pre-18S rRNA in Xenopus oocytes. RNA 1998, 4: 195-204. PMID: 9570319, PMCID: PMC1369608.Peer-Reviewed Original Research
1997
Functional separation of pre-rRNA processing steps revealed by truncation of the U3 small nucleolar ribonucleoprotein component, Mpp10
Lee S, Baserga S. Functional separation of pre-rRNA processing steps revealed by truncation of the U3 small nucleolar ribonucleoprotein component, Mpp10. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 13536-13541. PMID: 9391061, PMCID: PMC28341, DOI: 10.1073/pnas.94.25.13536.Peer-Reviewed Original ResearchMpp10p, 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 ResearchMeSH KeywordsAnimalsHumansMiceMutagenesis, Site-DirectedPhosphoproteinsRibonucleoproteinsRibonucleoproteins, Small NuclearRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, Ribosomal, 18SSaccharomyces cerevisiaeConceptsPre-rRNA processingNew protein componentsU3 snoRNPProtein componentsU3 small nucleolar ribonucleoproteinSmall nucleolar ribonucleoproteinEssential genesSlow growthConditional promoterU3 snoRNAMpp10pNucleolar ribonucleoproteinRRNA precursorProcessing eventsYeastSnoRNPsMpp10ProteinModel systemDegrees C. AnalysisC. AnalysisSnoRNAsMutantsRibonucleoproteinSaccharomyces
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 ResearchMeSH KeywordsAnimalsBase SequenceMolecular Sequence DataOocytesRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, RibosomalRNA, Small NuclearXenopus laevis
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 ResearchMeSH KeywordsBase SequenceCodonDNA, RecombinantGenesGlobinsHumansMutationRNA Processing, Post-TranscriptionalRNA, MessengerConceptsHeterologous 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 ResearchMeSH KeywordsBase SequenceCell LineHumansLeukemiaMitochondriaPoly ARNA Processing, Post-TranscriptionalRNA, Ribosomal