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
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 Research
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-Binding ProteinsRNA, FungalRNA, MessengerSaccharomyces 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
1993
Discrete 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
A 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: 3809-3818. 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