2011
The zipcode-binding protein ZBP1 influences the subcellular location of the Ro 60-kDa autoantigen and the noncoding Y3 RNA
Sim S, Yao J, Weinberg DE, Niessen S, Yates JR, Wolin SL. The zipcode-binding protein ZBP1 influences the subcellular location of the Ro 60-kDa autoantigen and the noncoding Y3 RNA. RNA 2011, 18: 100-110. PMID: 22114317, PMCID: PMC3261732, DOI: 10.1261/rna.029207.111.Peer-Reviewed Original ResearchConceptsY3 RNASubcellular locationCRM1 inhibitor leptomycin B.RNA-binding proteinExport signalVertebrate nucleiVertebrate cellsY RNAsRNA bindingLeptomycin B.Nuclear exportSubcellular localizationNoncoding RNAsRNA complexZBP1Ro proteinCellular componentsRNACytoplasmProteinNucleusCRM1Complex increasesExportUV irradiationAn intrinsically disordered C terminus allows the La protein to assist the biogenesis of diverse noncoding RNA precursors
Kucera NJ, Hodsdon ME, Wolin SL. An intrinsically disordered C terminus allows the La protein to assist the biogenesis of diverse noncoding RNA precursors. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 1308-1313. PMID: 21212361, PMCID: PMC3029687, DOI: 10.1073/pnas.1017085108.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnticodonChymotrypsinElectrophoretic Mobility Shift AssayImmunoblottingModels, MolecularMolecular Sequence DataMutationNucleic Acid ConformationProtein BindingProtein Structure, TertiaryRNA PrecursorsRNA, FungalRNA, RibosomalRNA, Small NuclearRNA, TransferRNA, UntranslatedRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTrypsin
2006
Molecular Chaperones and Quality Control in Noncoding RNA Biogenesis
WOLIN S, WURTMANN E. Molecular Chaperones and Quality Control in Noncoding RNA Biogenesis. Cold Spring Harbor Symposia On Quantitative Biology 2006, 71: 505-511. PMID: 17381333, DOI: 10.1101/sqb.2006.71.051.Peer-Reviewed Original ResearchConceptsRNA quality controlNoncoding RNAsMolecular chaperonesSm-like protein HfqQuality control pathwaysRNA biogenesisProtein HfqCorrect foldingEfficient foldingAnimal cellsExonucleolytic degradationLikely functionsLa proteinControl pathwaysQuality control systemRo proteinRNACertain bacteriaProteinChaperonesCritical roleFoldingFunctional structureBacteriaQuality control
2001
Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization.
Long K, Cedervall T, Walch-Solimena C, Noe D, Huddleston M, Annan R, Wolin S. Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization. RNA 2001, 7: 1589-602. PMID: 11720288, PMCID: PMC1370201.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensBinding SitesCell NucleolusCell NucleusFungal ProteinsMolecular Sequence DataPeptide MappingPhosphorylationProtein IsoformsRibonucleoproteinsRibonucleoproteins, Small NuclearRNARNA StabilityRNA, FungalRNA, TransferRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsLa proteinAbundant nuclear phosphoproteinRNA polymerase III transcriptsS. cerevisiae proteinTwo-dimensional gel electrophoresisRole of phosphorylationPolymerase III transcriptsCerevisiae proteinsNascent RNANascent transcriptsS. pombeSchizosaccharomyces pombeLhp1pPhosphorylation sitesYeast SaccharomycesProtein functionMutant versionSubcellular locationFirst proteinHuman proteinsNuclear phosphoproteinExonucleolytic degradationSerine phosphorylationPhosphorylation statusRNA stabilizationMultiple Functional Interactions Between Components of the Lsm2-Lsm8 Complex, U6 snRNA, and the Yeast La Protein
Pannone B, Do Kim S, Noe D, Wolin S. Multiple Functional Interactions Between Components of the Lsm2-Lsm8 Complex, U6 snRNA, and the Yeast La Protein. Genetics 2001, 158: 187-196. PMID: 11333229, PMCID: PMC1461625, DOI: 10.1093/genetics/158.1.187.Peer-Reviewed Original ResearchConceptsU6 snRNALa proteinLow copy suppressorU6 small nuclear ribonucleoproteinYeast La proteinSm-like proteinsFunctional interactionOnly essential functionU6 snRNA genesSmall nuclear ribonucleoproteinMultiple functional interactionsLsm geneRNA biogenesisLsm proteinsSnRNA genesEukaryotic spliceosomeSmall RNAsSm motifsAbundant phosphoproteinLsm8pU6 snRNPsFirst proteinNuclear ribonucleoproteinLhp1pSnRNA
2000
U snRNP assembly in yeast involves the La protein
Xue D, Rubinson D, Pannone B, Yoo C, Wolin S. U snRNP assembly in yeast involves the La protein. The EMBO Journal 2000, 19: 1650-1660. PMID: 10747032, PMCID: PMC310233, DOI: 10.1093/emboj/19.7.1650.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceDNA PrimersFungal ProteinsGenes, FungalMutationProtein BindingRibonucleoprotein, U1 Small NuclearRibonucleoprotein, U4-U6 Small NuclearRibonucleoproteins, Small NuclearRNA PrecursorsRNA StabilityRNA, FungalRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpliceosomesConceptsU4 RNALa proteinU4/U6 snRNPLa autoantigen bindsU snRNP assemblyRNA polymerase III transcriptsU4/U6 snRNPsRNA polymerase IIPolymerase III transcriptsEukaryotic nucleusSnRNP assemblySpliceosomal snRNPsSm proteinsU5 snRNPsMature RNAPolymerase IIU5 RNALhp1pU6 snRNPMutant cellsU6 snRNPsPermissive temperatureYeast cellsSnRNPsRNA
1999
Two Yeast La Motif-containing Proteins Are RNA-binding Proteins that Associate with Polyribosomes
Sobel S, Wolin S. Two Yeast La Motif-containing Proteins Are RNA-binding Proteins that Associate with Polyribosomes. Molecular Biology Of The Cell 1999, 10: 3849-3862. PMID: 10564276, PMCID: PMC25684, DOI: 10.1091/mbc.10.11.3849.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensFungal ProteinsGene DeletionGene Expression Regulation, FungalMicrofilament ProteinsMolecular Sequence DataPhylogenyPolyribosomesProtein BiosynthesisProtein Synthesis InhibitorsRibonucleoproteinsRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentConceptsRNA-binding proteinLa proteinRNA polymerase III transcriptsMotif-containing proteinsSaccharomyces cerevisiae proteinsPolymerase III transcriptsWild-type strainCerevisiae proteinsLa motifProtein synthesis inhibitorU6 RNASro9pIndirect immunofluorescence microscopyMRNA translationImmunofluorescence microscopyLhp1pEssential processProteinSynthesis inhibitorNormal pathwayDeletionMotifLHP1SLF1RibosomesThe trials and travels of tRNA
Wolin S, Matera A. The trials and travels of tRNA. Genes & Development 1999, 13: 1-10. PMID: 9887094, DOI: 10.1101/gad.13.1.1.Peer-Reviewed Original Research
1998
A role for the yeast La protein in U6 snRNP assembly: evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts
Pannone B, Xue D, Wolin S. A role for the yeast La protein in U6 snRNP assembly: evidence that the La protein is a molecular chaperone for RNA polymerase III transcripts. The EMBO Journal 1998, 17: 7442-7453. PMID: 9857199, PMCID: PMC1171088, DOI: 10.1093/emboj/17.24.7442.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensFungal ProteinsGene DosageMolecular ChaperonesMolecular Sequence DataMutationN-Terminal Acetyltransferase CRibonucleoprotein, U4-U6 Small NuclearRibonucleoproteinsRibonucleoproteins, Small NuclearRNA Polymerase IIIRNA PrecursorsRNA, FungalRNA, MessengerRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSnRNP Core ProteinsConceptsU6 snRNP assemblyPolymerase III transcriptsRNA polymerase III transcriptsSnRNP assemblyU6 snRNPLa proteinMolecular chaperonesYeast La proteinSm-like proteinsCore Sm proteinsFamily of proteinsSm proteinsU5 snRNPsU6 RNALhp1pFirst proteinPolymerase IIILa autoantigenNovel componentYeast cellsSnRNPEarly stepsLsm8pProteinTranscripts
1997
The La protein in Schizosaccharomyces pombe: a conserved yet dispensable phosphoprotein that functions in tRNA maturation.
Van Horn D, Yoo C, Xue D, Shi H, Wolin S. The La protein in Schizosaccharomyces pombe: a conserved yet dispensable phosphoprotein that functions in tRNA maturation. RNA 1997, 3: 1434-43. PMID: 9404894, PMCID: PMC1369584.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensCarrier ProteinsCytoskeletal ProteinsFungal ProteinsHumansMolecular Sequence DataPhosphoproteinsPhosphorylationRecombinant Fusion ProteinsRestriction MappingRibonucleoproteinsRNA Processing, Post-TranscriptionalRNA, FungalRNA, TransferRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSequence Homology, Amino AcidConceptsLa proteinAbundant nuclear phosphoproteinRNA polymerase III transcriptsFission yeast SchizosaccharomycesPre-tRNA maturationS. pombe cellsPolymerase III transcriptsWild-type cellsHuman La proteinYeast SchizosaccharomycesS. pombePombe cellsYeast SaccharomycesTRNA precursorsNuclear phosphoproteinPattern of tRNAS. cerevisiaeLa autoantigenTRNAProteinSchizosaccharomycesPhosphoproteinYeastExhibit alterationsMaturationThe Yeast La Protein Is Required for the 3′ Endonucleolytic Cleavage That Matures tRNA Precursors
Yoo C, Wolin S. The Yeast La Protein Is Required for the 3′ Endonucleolytic Cleavage That Matures tRNA Precursors. Cell 1997, 89: 393-402. PMID: 9150139, DOI: 10.1016/s0092-8674(00)80220-2.Peer-Reviewed Original ResearchMeSH KeywordsAutoantigensBase CompositionCell DivisionEndonucleasesExonucleasesFungal ProteinsGene Expression Regulation, EnzymologicGene Expression Regulation, FungalMolecular Sequence DataMutationNucleic Acid ConformationRibonucleoproteinsRNA PrecursorsRNA, Transfer, SerRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsConceptsTrailer sequencesEndonucleolytic cleavageLa autoantigen bindsYeast La proteinPolymerase III transcriptsS. cerevisiae cellsEndonucleolytic removalLhp1pTRNA precursorsLa proteinCerevisiae cellsAnticodon stemSecond mutationMutationsCellsCleavageTranscriptsProteinBindsSequenceMaturationStemConformation
1996
A misfolded form of 5S rRNA is complexed with the Ro and La autoantigens.
Shi H, O'Brien C, Van Horn D, Wolin S. A misfolded form of 5S rRNA is complexed with the Ro and La autoantigens. RNA 1996, 2: 769-84. PMID: 8752087, PMCID: PMC1369414.Peer-Reviewed Original ResearchConceptsRRNA precursorRo proteinAlternative helixQuality control pathwaysYeast Saccharomyces cerevisiaeSmall cytoplasmic RNAProtein-protein interactionsOligonucleotide-directed RNase H cleavageWild-type precursorRRNA biosynthesisY RNAsSecondary structure determinantsMutant RNAsSaccharomyces cerevisiaeLa proteinControl pathwaysCytoplasmic RNANuclease digestionInternal mutationsRRNARNAXenopus oocytesProteinSimilar sequencesRo autoantigen
1994
La proteins from Drosophila melanogaster and Saccharomyces cerevisiae: a yeast homolog of the La autoantigen is dispensable for growth.
Yoo C, Wolin S. La proteins from Drosophila melanogaster and Saccharomyces cerevisiae: a yeast homolog of the La autoantigen is dispensable for growth. Molecular And Cellular Biology 1994, 14: 5412-5424. PMID: 8035818, PMCID: PMC359060, DOI: 10.1128/mcb.14.8.5412.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAutoantigensBase SequenceChromosome MappingCloning, MolecularDNA PrimersDrosophila melanogasterFungal ProteinsGenes, FungalGenes, InsectMolecular Sequence DataMutagenesis, InsertionalNuclear ProteinsPlant ProteinsRibonucleoproteinsRNA Polymerase IIIRNA, Ribosomal, 5SRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino AcidConceptsLa proteinDrosophila melanogasterYeast La proteinRNA polymerase IIIPolymerase III transcriptsHuman La proteinYeast homologTranscription extractProtein homologsYeast proteinsVertebrate speciesYeast SaccharomycesProtein functionRedundant rolesHuman proteinsPolymerase IIISaccharomyces cerevisiaeLa autoantigenNull allelesGenetic analysisYeast cellsDrosophilaAutoantigen LaHomologBiochemical properties