2011
An 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
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
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 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
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 pathwayDeletionMotifLHP1SLF1Ribosomes
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 alterationsMaturation
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
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
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 cytoplasmRibonucleoprotein
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: 3801-3808. 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