2004
Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patch
Dong G, Chakshusmathi G, Wolin SL, Reinisch KM. Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patch. The EMBO Journal 2004, 23: 1000-1007. PMID: 14976553, PMCID: PMC380972, DOI: 10.1038/sj.emboj.7600115.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsAutoantigensConserved SequenceCrystallography, X-RayHelix-Turn-Helix MotifsHydroxylationModels, MolecularMolecular Sequence DataMutationPhosphatesProtein BindingProtein Structure, TertiaryRibonucleoproteinsRNASequence AlignmentSubstrate SpecificityTrypanosoma brucei bruceiConceptsLa motifLa proteinRNA polymerase III transcriptsFirst structural insightsRNA-binding proteinPolymerase III transcriptsHelix domainNuclear phosphoproteinRNA substratesMutagenesis experimentsStructural insightsConserved regionsHigh-affinity bindingAromatic patchHelix architectureProteinSurface residuesMotifRNAUridylateCritical roleTranscriptsPhosphoproteinExonucleaseFolding
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
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
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 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
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 assembliesRNATranscripts
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 propertiesLa 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. DOI: 10.1128/mcb.14.8.5412-5424.1994.Peer-Reviewed Original ResearchLa 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 propertiesRNA polymerase III-mediated transcription of the trypanosome U2 small nuclear RNA gene is controlled by both intragenic and extragenic regulatory elements.
Fantoni A, Dare A, Tschudi C. RNA polymerase III-mediated transcription of the trypanosome U2 small nuclear RNA gene is controlled by both intragenic and extragenic regulatory elements. Molecular And Cellular Biology 1994, 14: 2021-2028. PMID: 8114733, PMCID: PMC358562, DOI: 10.1128/mcb.14.3.2021.Peer-Reviewed Original ResearchMeSH KeywordsAmanitinsAnimalsBase SequenceConsensus SequenceDNA, ProtozoanGenes, ProtozoanMolecular Sequence DataPromoter Regions, GeneticRegulatory Sequences, Nucleic AcidRNA Polymerase IIIRNA, Small NuclearSequence AlignmentSequence DeletionSequence Homology, Nucleic AcidTranscription, GeneticTrypanosomaConceptsU2 small nuclear RNA genesSmall nuclear RNA genesNuclear RNA genesU2 snRNA genesSnRNA genesRNA genesCis-acting regulatory sequencesRNA polymerase III transcriptsInsect form trypanosomesSnRNA gene expressionRNA polymerase IIInternal control regionRNA polymerase IIIPolymerase III transcriptsTranscription start siteIII-like enzymeTRNA genesPolymerase IIRNA polymeraseRegulatory sequencesU2 snRNAControl regionPolymerase IIIStart siteRegulatory elementsRNA Polymerase III-Mediated Transcription of the Trypanosome U2 Small Nuclear RNA Gene Is Controlled by both Intragenic and Extragenic Regulatory Elements
Fantoni A, Dare A, Tschudi C. RNA Polymerase III-Mediated Transcription of the Trypanosome U2 Small Nuclear RNA Gene Is Controlled by both Intragenic and Extragenic Regulatory Elements. Molecular And Cellular Biology 1994, 14: 2021-2028. DOI: 10.1128/mcb.14.3.2021-2028.1994.Peer-Reviewed Original ResearchU2 small nuclear RNA genesSmall nuclear RNA genesNuclear RNA genesU2 snRNA genesSnRNA genesRNA genesRNA polymeraseCis-acting regulatory sequencesRNA polymerase III transcriptsInsect form trypanosomesSnRNA gene expressionRNA polymerase IIInternal control regionPolymerase III transcriptsTranscription start siteIII-like enzymeTRNA genesPolymerase IIRegulatory sequencesU2 snRNAControl regionStart siteRegulatory elementsPromoter elementsMutant constructs
1989
The RNA binding protein La influences both the accuracy and the efficiency of RNA polymerase III transcription in vitro.
Gottlieb E, Steitz JA. The RNA binding protein La influences both the accuracy and the efficiency of RNA polymerase III transcription in vitro. The EMBO Journal 1989, 8: 841-850. PMID: 2498086, PMCID: PMC400883, DOI: 10.1002/j.1460-2075.1989.tb03445.x.Peer-Reviewed Original ResearchConceptsTranscription levelsNascent RNA polymerase III transcriptsRNA polymerase III transcriptionAbundant nuclear phosphoproteinRNA polymerase III transcriptsPolymerase III transcriptionPolymerase III transcriptsClass III genesHeLa cell extractsAction of LaTranscript lengthTermination signalNuclear phosphoproteinUridylate residuesLa proteinTranscription activityAutoantigen LaCell extractsTranscriptsRNAAbsence of LAMouse monoclonal antibodyTranscriptionPhosphoproteinGenes
1981
Ro small cytoplasmic ribonucleoproteins are a subclass of La ribonucleoproteins: further characterization of the Ro and La small ribonucleoproteins from uninfected mammalian cells.
Hendrick JP, Wolin SL, Rinke J, Lerner MR, Steitz JA. Ro small cytoplasmic ribonucleoproteins are a subclass of La ribonucleoproteins: further characterization of the Ro and La small ribonucleoproteins from uninfected mammalian cells. Molecular And Cellular Biology 1981, 1: 1138-1149. PMID: 6180298, PMCID: PMC369740, DOI: 10.1128/mcb.1.12.1138.Peer-Reviewed Original ResearchConceptsLa RNAsHuman cellsRNA polymerase III transcriptsNuclear transcription systemRNA polymerase IIIUninfected mammalian cellsPolymerase III transcriptsSmall cytoplasmic ribonucleoproteinsDifferent RNA moleculesSmall ribonucleic acidsProtein complexesSmall ribonucleoproteinTransfer RNAMammalian cellsRo RNPsPolymerase IIIRNA componentCytoplasmic ribonucleoproteinRNA moleculesTranscription systemMouse cellsReconstitution experimentsRNARNA-like moleculesCell cytoplasmRo Small Cytoplasmic Ribonucleoproteins Are a Subclass of La Ribonucleoproteins: Further Characterization of the Ro and La Small Ribonucleoproteins from Uninfected Mammalian Cells
Hendrick J, Wolin S, Rinke J, Lerner M, Steitz J. Ro Small Cytoplasmic Ribonucleoproteins Are a Subclass of La Ribonucleoproteins: Further Characterization of the Ro and La Small Ribonucleoproteins from Uninfected Mammalian Cells. Molecular And Cellular Biology 1981, 1: 1138-1149. DOI: 10.1128/mcb.1.12.1138-1149.1981.Peer-Reviewed Original ResearchLa RNAsHuman cellsRNA polymerase III transcriptsNuclear transcription systemRNA polymerase IIIUninfected mammalian cellsPolymerase III transcriptsSmall cytoplasmic ribonucleoproteinsDifferent RNA moleculesSmall ribonucleic acidsProtein complexesSmall ribonucleoproteinTransfer RNAMammalian cellsRo RNPsPolymerase IIIRNA componentCytoplasmic ribonucleoproteinRNA moleculesTranscription systemMouse cellsReconstitution experimentsLa ribonucleoproteinsRibonucleoproteinRNA
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