2023
CLIP-Seq analysis enables the design of protective ribosomal RNA bait oligonucleotides against C9ORF72 ALS/FTD poly-GR pathophysiology
Ortega J, Sasselli I, Boccitto M, Fleming A, Fortuna T, Li Y, Sato K, Clemons T, Mckenna E, Nguyen T, Anderson E, Asin J, Ichida J, Pandey U, Wolin S, Stupp S, Kiskinis E. CLIP-Seq analysis enables the design of protective ribosomal RNA bait oligonucleotides against C9ORF72 ALS/FTD poly-GR pathophysiology. Science Advances 2023, 9: eadf7997. PMID: 37948524, PMCID: PMC10637751, DOI: 10.1126/sciadv.adf7997.Peer-Reviewed Original Research
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
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
2000
RNA degradation: Sm-like proteins wRING the neck of mRNA
Pannone B, Wolin S. RNA degradation: Sm-like proteins wRING the neck of mRNA. Current Biology 2000, 10: r478-r481. PMID: 10898971, DOI: 10.1016/s0960-9822(00)00552-2.Peer-Reviewed Original ResearchRo 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 ResearchImport of proteins into the trypanosome nucleus and their distribution at karyokinesis
Marchetti M, Tschudi C, Kwon H, Wolin S, Ullu E. Import of proteins into the trypanosome nucleus and their distribution at karyokinesis. Journal Of Cell Science 2000, 113: 899-906. PMID: 10671379, DOI: 10.1242/jcs.113.5.899.Peer-Reviewed Original ResearchConceptsNuclear localization sequenceMonopartite nuclear localization sequenceBipartite nuclear localization sequenceFusion proteinSpecific nuclear localization sequencesImport of proteinsEarly divergent eukaryoteGreen fluorescent proteinDivergent eukaryotesOrganism's proteinsChromosome segregationBeta-galactosidase reporterTrypanosomatid protozoaProtein homologueTrypanosomal proteinsHistone H2BHistone H2B.Localization sequenceNuclear divisionLa proteinC-terminusTrypanosome nucleusMitotic cellsFluorescent proteinATP synthesis
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
Caenorhabditis 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
1988
Ribosome pausing and stacking during translation of a eukaryotic mRNA.
Wolin S, Walter P. Ribosome pausing and stacking during translation of a eukaryotic mRNA. The EMBO Journal 1988, 7: 3559-3569. PMID: 2850168, PMCID: PMC454858, DOI: 10.1002/j.1460-2075.1988.tb03233.x.Peer-Reviewed Original Research
1987
Nuclear lamin LI of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily.
Krohne G, Wolin S, McKeon F, Franke W, Kirschner M. Nuclear lamin LI of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily. The EMBO Journal 1987, 6: 3801-8. PMID: 3428276, PMCID: PMC553852, DOI: 10.1002/j.1460-2075.1987.tb02716.x.Peer-Reviewed Original ResearchConceptsAmino acid sequenceLamin LIAcid sequenceIdentical amino acid positionsLong C-terminal tailDetailed sequence comparisonXenopus laevisC-terminal tailNear-neutral pIAmino acid positionsIntermediate filament proteinsHuman lamin A.Karyoskeletal proteinsLamin BCDNA clonesCoil domainHelical domainSequence comparisonXenopus laminLamin ALamin B.CDNA cloningLamin A.LaminsNuclear envelopeA new lamin in Xenopus somatic tissues displays strong homology to human lamin A.
Wolin S, Krohne G, Kirschner M. A new lamin in Xenopus somatic tissues displays strong homology to human lamin A. The EMBO Journal 1987, 6: 3809-18. PMID: 3428277, PMCID: PMC553853, DOI: 10.1002/j.1460-2075.1987.tb02717.x.Peer-Reviewed Original ResearchConceptsHuman lamin ACDNA clonesXenopus laminSomatic tissuesLamin AMajor lamin proteinsCarboxy-terminal domainAdult somatic cellsHuman lamin A.Major laminsDistinct structural classesLamin proteinsNuclear laminaLamin LIIIEmbryonic developmentSomatic cellsSomatic laminsStrong homologyLamin A.Lamin LILaminsMajor polypeptidesGerm cellsProteinClones