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
2001
Multiple 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 cellsSnRNPsRNARo 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
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 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 properties
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
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 envelope
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 extractsGenesRNAGenomeRNAsHY3CellsMY1
1980
Are snRNPs involved in splicing?
Lerner M, Boyle J, Mount S, Wolin S, Steitz J. Are snRNPs involved in splicing? Nature 1980, 283: 220-224. PMID: 7350545, DOI: 10.1038/283220a0.Peer-Reviewed Original ResearchConceptsSmall nuclear RNA speciesProminent nuclear proteinsRNA-protein complexesSmall RNA moleculesSmall nuclear ribonucleoproteinNuclear RNA speciesSnRNA speciesSnRNAs U1RNA speciesU6 RNASnRNA moleculesNuclear proteinsNuclear ribonucleoproteinNucleotide sequenceU1 RNARNA moleculesSnRNPsExtensive complementaritySplice junctionsNuclear locationLines of evidenceAnti-Sm seraCell nucleiHnRNA moleculesMouse Ehrlich