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-Binding ProteinsRNA, FungalRNA, RibosomalRNA, Small NuclearRNA, TransferRNA, UntranslatedSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTrypsin
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-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
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
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
1987
A Subset of Yeast snRNA's Contains Functional Binding Sites for the Highly Conserved Sm Antigen
Riedel N, Wolin S, Guthrie C. A Subset of Yeast snRNA's Contains Functional Binding Sites for the Highly Conserved Sm Antigen. Science 1987, 235: 328-331. PMID: 2948278, DOI: 10.1126/science.2948278.Peer-Reviewed Original Research