2018
Bacterial Y RNAs: Gates, Tethers, and tRNA Mimics
Sim S, Wolin S. Bacterial Y RNAs: Gates, Tethers, and tRNA Mimics. 2018, 369-381. DOI: 10.1128/9781683670247.ch21.Peer-Reviewed Original ResearchY RNAsBacterial Y RNAsRing-shaped proteinSubset of bacteriaCharacterized organismsProtein partnersNoncoding RNAsTRNA mimicAnimal cellsHomology searchHuman RNAHuman cellsRNANucleotidesImportant targetBacteriaSystemic autoimmune rheumatic diseasesAutoimmune rheumatic diseasesSystemic lupus erythematosusCellsRNAsOrganismsSpeciesProteinLupus erythematosus
2015
A retrovirus packages nascent host noncoding RNAs from a novel surveillance pathway
Eckwahl MJ, Sim S, Smith D, Telesnitsky A, Wolin SL. A retrovirus packages nascent host noncoding RNAs from a novel surveillance pathway. Genes & Development 2015, 29: 646-657. PMID: 25792599, PMCID: PMC4378196, DOI: 10.1101/gad.258731.115.Peer-Reviewed Original ResearchConceptsSmall nuclear RNAMoloney leukemia virusSurveillance pathwayU6 small nuclear RNASmall nucleolar RNAsHigh-throughput sequencingHost cell RNAExoribonuclease DIS3L2RNA exosomeLeukemia virusExportin-5Nucleolar RNAsNuclear RNAHost RNASpecific tRNAsCytoplasmic recruitmentMurine leukemia virusCell RNAEndogenous retrovirusesRNAModel retrovirusRNAsVirionsCytoplasmPathway
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
2012
Nuclear noncoding RNA surveillance: is the end in sight?
Wolin SL, Sim S, Chen X. Nuclear noncoding RNA surveillance: is the end in sight? Trends In Genetics 2012, 28: 306-313. PMID: 22475369, PMCID: PMC3378728, DOI: 10.1016/j.tig.2012.03.005.Peer-Reviewed Original ResearchConceptsRNA surveillance pathwaySurveillance pathwayAberrant RNAsSteady-state transcriptomeYeast counterpartEukaryotic cellsProtein cofactorsMammalian cellsRNA determinantsHuman diseasesSubsequent degradationRNACofactorPathwayKey roleRecent studiesMetazoansExoribonucleasesAccessible endTranscriptomeNcRNAsCellsYeastNucleaseProtein
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-Binding ProteinsRNA, FungalRNA, RibosomalRNA, Small NuclearRNA, TransferRNA, UntranslatedSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTrypsin
2008
Running Rings Around RNA: The role of Ro RNPs in RNA maturation and decay
Wolin S. Running Rings Around RNA: The role of Ro RNPs in RNA maturation and decay. The FASEB Journal 2008, 22: 527.3-527.3. DOI: 10.1096/fasebj.22.1_supplement.527.3.Peer-Reviewed Original ResearchY RNAsRNA bindsAnimal cellsRNA binding proteinRNA quality controlY-RNAsRo RNPsRNA maturationVertebrate cellsSmall RNAsCertain prokaryotesMammalian cellsD. radioduransLikely functionsStructured RNAsRunning ringsHelical portionBinding proteinRNABiochemical studiesEfficient maturationCentral cavityBacteriaProteinBinds
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
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-Binding ProteinsRNA, FungalSaccharomyces 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
Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle
Seto A, Zaug A, Sobel S, Wolin S, Cech T. Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle. Nature 1999, 401: 177-180. PMID: 10490028, DOI: 10.1038/43694.Peer-Reviewed Original ResearchConceptsSm proteinsSaccharomyces cerevisiae telomeraseNuclear messenger RNASmall nuclear ribonucleoprotein particleRNA polymerase IISmall nuclear ribonucleoproteinNuclear ribonucleoprotein particleTrimethylguanosine capPolymerase IIRNA processingTelomerase RNAEnzyme telomeraseNuclear ribonucleoproteinRibonucleoprotein particleProtein subunitsMessenger RNATelomeraseTelomerase activityRNAProteinEukaryotesSnRNPsYeast extractRibonucleoproteinChromosomes
1998
Binding 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
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 roleVertebratesRNPsNucleotides
1985
Small cytoplasmic ribonucleoproteins
Wolin S. Small cytoplasmic ribonucleoproteins. Trends In Genetics 1985, 1: 201-204. DOI: 10.1016/0168-9525(85)90080-0.Peer-Reviewed Original Research
1983
Genes for two small cytoplasmic Ro RNAs are adjacent and appear to be single-copy in the human genome
Wolin S, Steitz J. Genes for two small cytoplasmic Ro RNAs are adjacent and appear to be single-copy in the human genome. Cell 1983, 32: 735-744. PMID: 6187471, DOI: 10.1016/0092-8674(83)90059-4.Peer-Reviewed Original ResearchConceptsHuman genomeRo RNAsSecondary structure homologyRNA polymerase IIISmall cytoplasmic ribonucleoproteinsClass III genesGenomic clonesMammalian cellsPolymerase IIIRNA componentStructure homologySingle copyCytoplasmic ribonucleoproteinHY5 RNAMouse cellsHuman cellsHY1Cell extractsGenesRNAGenomeRNAsHY3CellsMY1Structure and Function of Small Ribonucleoproteins from Eukaryotic Cells
Steitz JA, Berg C, Gottlieb E, Hardin JA, Hashimoto C, Hendrick JP, Hinterberger M, Krikeles M, Lerner MR, Mount SM, Pettersson I, Rinke J, Rosa M, Wolin S. Structure and Function of Small Ribonucleoproteins from Eukaryotic Cells. 1983, 12: 309-317. PMID: 7166547, DOI: 10.1016/b978-0-12-501650-6.50023-7.Peer-Reviewed Original ResearchConceptsSmall ribonucleoproteinLa proteinRNA polymerase III transcription factorSmall RNA-protein complexesDrosophila U1 RNAU1 small nuclearRNA-protein complexesHnRNA splicingEukaryotic cellsSmall cytoplasmicMammalian cellsRRNA precursorTranscription factorsSmall nuclearU1 RNASplice junctionsRibonucleoproteinLa ribonucleoproteinsFurther characterizationProteinRelated diseasesCellsSplicingTRNARNA
1982
Small RNPs in eucaryotic cells
Hendrick J, Mount S, Rinke J, Wolin S, Rosa M, Gottlieb E, Lerner M, Steitz J. Small RNPs in eucaryotic cells. 1982, 321-328. DOI: 10.1007/978-1-349-06343-7_44.Peer-Reviewed Original ResearchSmall nuclear RNAAbundant small nuclear RNAsRNA-protein complexesEukaryotic cellsSmall RNAsSmall ribonucleoproteinSubcellular locationNuclear RNARNA componentU1 snRNPsEucaryotic cellsComponent RNARibonucleoproteinRNP particlesRNAInitial discoveryProteinPartial characterizationState of maturationSnRNPsCellsSystemic lupus erythematosusDiversityMaturationMetabolism