2014
Bacterial noncoding Y RNAs are widespread and mimic tRNAs
Chen X, Sim S, Wurtmann EJ, Feke A, Wolin SL. Bacterial noncoding Y RNAs are widespread and mimic tRNAs. RNA 2014, 20: 1715-1724. PMID: 25232022, PMCID: PMC4201824, DOI: 10.1261/rna.047241.114.Peer-Reviewed Original ResearchConceptsY RNAsStructured RNA degradationRing-shaped proteinNoncoding Y RNAsBacterial physiologyAnimal cellsNucleotide modificationsDeinococcus radioduransPhage speciesRNA degradationTRNARo60 autoantigenRNAOrthologsNcRNAsSpeciesBacteriaExoribonucleaseRNAsRadioduransProteinRo60EnzymePhysiologyPhosphorylase
2013
An RNA Degradation Machine Sculpted by Ro Autoantigen and Noncoding RNA
Chen X, Taylor DW, Fowler CC, Galan JE, Wang HW, Wolin SL. An RNA Degradation Machine Sculpted by Ro Autoantigen and Noncoding RNA. Cell 2013, 153: 166-177. PMID: 23540697, PMCID: PMC3646564, DOI: 10.1016/j.cell.2013.02.037.Peer-Reviewed Original ResearchConceptsRNA degradation machineDegradation machineY RNAsSingle-particle electron microscopyRing-shaped proteinRibosomal RNA maturationExoribonuclease polynucleotide phosphorylaseRo autoantigenNcRNAs actRRNA decayRNA maturationProtein cofactorsNoncoding RNAsSubstrate specificityDeinococcus radioduransStructured RNAsPolynucleotide phosphorylaseBiochemical assaysRNAOrthologsNcRNAPNPaseProteinSalmonella typhimuriumAtomic model
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 irradiation
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 stabilization
2000
Ro ribonucleoproteins contribute to the resistance of Deinococcus radiodurans to ultraviolet irradiation
Chen X, Quinn A, Wolin S. Ro ribonucleoproteins contribute to the resistance of Deinococcus radiodurans to ultraviolet irradiation. Genes & Development 2000, 14: 777-782. PMID: 10766734, PMCID: PMC316496, DOI: 10.1101/gad.14.7.777.Peer-Reviewed Original Research
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 stepsLsm8pProteinTranscriptsBinding of the 60-kDa Ro autoantigen to Y RNAs: evidence for recognition in the major groove of a conserved helix.
Green C, Long K, Shi H, Wolin S. Binding of the 60-kDa Ro autoantigen to Y RNAs: evidence for recognition in the major groove of a conserved helix. RNA 1998, 4: 750-65. PMID: 9671049, PMCID: PMC1369656, DOI: 10.1017/s1355838298971667.Peer-Reviewed Original ResearchConceptsY RNAsSpecific base pairsRo proteinRRNA precursorConserved helixMajor grooveBase pairsSmall cytoplasmic RNAThree-nucleotide bulgeProtein side chainsProtein bindsCytoplasmic RNARNA sequencesProtein recognitionRNAXenopus oocytesProteinHelixRo autoantigenDistinct classesDiethyl pyrocarbonateProtein bindingStructural alterationsSide chainsDimethyl sulfate
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
1995
A perinucleolar compartment contains several RNA polymerase III transcripts as well as the polypyrimidine tract-binding protein, hnRNP I.
Matera A, Frey M, Margelot K, Wolin S. A perinucleolar compartment contains several RNA polymerase III transcripts as well as the polypyrimidine tract-binding protein, hnRNP I. Journal Of Cell Biology 1995, 129: 1181-1193. PMID: 7539809, PMCID: PMC2120477, DOI: 10.1083/jcb.129.5.1181.Peer-Reviewed Original ResearchConceptsY RNAsPol III transcriptsPerinucleolar compartmentHnRNP I/PTBRNA polymerase III transcriptsGenomic DNA clonesPolypyrimidine tract-binding proteinHuman Y RNAsRNA polymerase IIIPolymerase III transcriptsTract-binding proteinRNase MRPRo RNPsNuclear subdomainsTranscription sitesNucleolar peripheryRNase PSubcellular organizationDNA clonesPolymerase IIIRNA componentGene locusMacromolecular assembliesRNATranscriptsCaenorhabditis elegans embryos contain only one major species of Ro RNP.
Van Horn D, Eisenberg D, O'Brien C, Wolin S. Caenorhabditis elegans embryos contain only one major species of Ro RNP. RNA 1995, 1: 293-303. PMID: 7489501, PMCID: PMC1369082.Peer-Reviewed Original ResearchConceptsY RNAsRo proteinRo RNPsC. elegans proteinsRNA recognition motifHuman Y RNAsN-terminal extensionPyrimidine-rich internal loopRo autoantigenRNP functionVertebrate proteinsDiscard pathwayVertebrate cellsC. elegansInvertebrate speciesNematode CaenorhabditisVertebrate speciesProtein functionHuman proteinsRNA biosynthesisDefective precursorsRecognition motifRNA moleculesGenetic analysisRNA
1994
A possible role for the 60-kD Ro autoantigen in a discard pathway for defective 5S rRNA precursors.
O'Brien C, Wolin S. A possible role for the 60-kD Ro autoantigen in a discard pathway for defective 5S rRNA precursors. Genes & Development 1994, 8: 2891-2903. PMID: 7995526, DOI: 10.1101/gad.8.23.2891.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutoantibodiesAutoantigensAutoimmune DiseasesBase SequenceDNA PrimersDNA, ComplementaryFemaleHumansMolecular Sequence DataMolecular WeightMutagenesisNucleic Acid ConformationOocytesOvaryPolymerase Chain ReactionRibonucleoproteinsRNA PrecursorsRNA, Ribosomal, 5SRNA, Small CytoplasmicTranscription, GeneticXenopusConceptsDiscard pathwayRRNA precursorCytoplasmic RNA-protein complexesRNA-protein complexesVariety of vertebratesRo autoantigenRo RNPsRRNA productionProtein bindsMutant RNAsRRNA sequencesMore point mutationsAdditional nucleotidesRo proteinRRNAPoint mutationsTerminal extensionXenopus oocytesProteinRNAPathwayPossible roleVertebratesRNPsNucleotidesLa 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 propertiesFrom the elephant to E. coli: SRP-dependent protein targeting
Wolin S. From the elephant to E. coli: SRP-dependent protein targeting. Cell 1994, 77: 787-790. PMID: 8004667, DOI: 10.1016/0092-8674(94)90124-4.Peer-Reviewed Original Research
1993
Xenopus Ro ribonucleoproteins: members of an evolutionarily conserved class of cytoplasmic ribonucleoproteins.
O'Brien C, Margelot K, Wolin S. Xenopus Ro ribonucleoproteins: members of an evolutionarily conserved class of cytoplasmic ribonucleoproteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 7250-7254. PMID: 7688474, PMCID: PMC47114, DOI: 10.1073/pnas.90.15.7250.Peer-Reviewed Original ResearchConceptsY RNAsRo proteinSmall ribonucleoproteinHuman Y RNAsSmall RNA moleculesXenopus egg extractsAmino acid sequenceY-RNAsHY3 RNAsVertebrate speciesMammalian cellsRo RNPsSubcellular locationRNA componentCytoplasmic ribonucleoproteinHY5 RNAAdditional proteinsRNA moleculesAcid sequenceHuman RNAEgg extractsEntire proteinConserved stemOocyte cytoplasmRibonucleoproteinDiscrete nascent chain lengths are required for the insertion of presecretory proteins into microsomal membranes.
Wolin S, Walter P. Discrete nascent chain lengths are required for the insertion of presecretory proteins into microsomal membranes. Journal Of Cell Biology 1993, 121: 1211-1219. PMID: 8389768, PMCID: PMC2119713, DOI: 10.1083/jcb.121.6.1211.Peer-Reviewed Original ResearchConceptsSignal recognition particlePresecretory proteinsER membraneInteraction of SRPSecretory proteinsNascent chain lengthNascent secretory proteinsMembrane-associated ribosomesTranslation of mRNAsMicrosomal membranesMembrane-bound ribosomesRecognition particleSmall ribonucleoproteinTranslation arrestSignal peptideRibosomesBovine preprolactinProteinHigh saltMembraneFurther elongationChain insertionPreprolactinRibonucleoproteinTranslation
1989
Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate.
Wolin S, Walter P. Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate. Journal Of Cell Biology 1989, 109: 2617-2622. PMID: 2556403, PMCID: PMC2115964, DOI: 10.1083/jcb.109.6.2617.Peer-Reviewed Original ResearchConceptsSignal recognition particleReticulocyte lysateRecognition particleMammalian signal recognition particleWheat germ translation extractsCanine pancreatic microsomal membranesTargeting of ribosomesPancreatic microsomal membranesWheat germ extractSRP bindsPresecretory proteinsElongation arrestER membraneTranslation arrestSignal sequenceTranslation extractsSecretory proteinsGerm extractRibosomesPreprolactin mRNAMicrosomal membranesLysatesSpecific sitesProteinFurther elongation