2008
Life without RNase P
Randau L, Schröder I, Söll D. Life without RNase P. Nature 2008, 453: 120-123. PMID: 18451863, DOI: 10.1038/nature06833.Peer-Reviewed Original Research
2005
Autoantibody Recognition of Macromolecular Structures and Their Subunits
Champion E, Baserga S. Autoantibody Recognition of Macromolecular Structures and Their Subunits. 2005, 379-417. DOI: 10.1002/3527607854.ch17.Peer-Reviewed Original ResearchSm monoclonal antibodyRNA polymerase IBox C/D small nucleolar RNAsPre-mRNA splicingRNase MRPSmall nucleolar RNAsRNase PPolymerase IU3 snoRNASubcellular localizationMolecular markersProtein componentsNucleolar RNAsHuman exosomeNew functionsPolymyositis-scleroderma overlap syndromeCurrent understandingSnRNPsSnoRNAsSplicingFibrillarinNucleolarMonoclonal antibodiesExosomesHUBF
1996
Association of RNase mitochondrial RNA processing enzyme with ribonuclease P in higher ordered structures in the nucleolus: a possible coordinate role in ribosome biogenesis.
Lee B, Matera AG, Ward DC, Craft J. Association of RNase mitochondrial RNA processing enzyme with ribonuclease P in higher ordered structures in the nucleolus: a possible coordinate role in ribosome biogenesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 11471-11476. PMID: 8876159, PMCID: PMC38081, DOI: 10.1073/pnas.93.21.11471.Peer-Reviewed Original ResearchConceptsMitochondrial RNA processing enzymeRibosomal RNA maturationRNA processing enzymesRNA maturationRibonuclease PRNase PProcessing enzymesSitu hybridization experimentsRNA structural motifsRibosome biogenesisRibosome assemblySmall subpopulationRibonucleoprotein particleRNA componentMacromolecular complexesRNA transcriptsHybridization experimentsFractionation experimentsCoordinate roleCytoplasmic structuresAffinity selectionEnzymeStructural motifsMethyl oligoribonucleotideNucleoli
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
1990
The RNA component of RNase P in Schizosaccharomyces species
Zimmerly S, Gamulin V, Burkard U, Söll D. The RNA component of RNase P in Schizosaccharomyces species. FEBS Letters 1990, 271: 189-193. PMID: 2226803, DOI: 10.1016/0014-5793(90)80403-6.Peer-Reviewed Original ResearchConceptsSchizosaccharomyces speciesS. pombeS. octosporusFission yeast SchizosaccharomycesSecondary structure modelComparative structural informationYeast SchizosaccharomycesGenes divergeRNase PRelated organismsSingle geneRNA componentNorthern analysisK RNAGenesS. japonicusSpeciesPombeOctosporusRNAStructural informationSequenceSchizosaccharomycesCopurifiesCloning
1989
An immunological determinant of RNase P protein is conserved between Escherichia coli and humans.
Mamula MJ, Baer M, Craft J, Altman S. An immunological determinant of RNase P protein is conserved between Escherichia coli and humans. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 8717-8721. PMID: 2479027, PMCID: PMC298359, DOI: 10.1073/pnas.86.22.8717.Peer-Reviewed Original ResearchThe RNA Processing Enzyme RNase MRP Is Identical to the Th RNP and Related to RNase P
Gold H, Topper J, Clayton D, Craft J. The RNA Processing Enzyme RNase MRP Is Identical to the Th RNP and Related to RNase P. Science 1989, 245: 1377-1380. PMID: 2476849, DOI: 10.1126/science.2476849.Peer-Reviewed Original ResearchConceptsRNA processing enzymesRNase MRPMitochondrial RNA processing enzymeProcessing enzymesRNase MRP activityHuman cell extractsNucleotide sequence analysisRNP enzymeEukaryotic cellsRibonuclease PBiochemical purificationRNase PRNA componentRNA transcriptsSequence analysisCell extractsRNPMRP activityEnzymeMRPTerminusMitochondriaTranscriptsPolypeptideBindsSubstrate structural requirements of Schizosaccharomyces pombe RNase P
Drainas D, Zimmerly S, Willis I, Söll D. Substrate structural requirements of Schizosaccharomyces pombe RNase P. FEBS Letters 1989, 251: 84-88. PMID: 2666172, DOI: 10.1016/0014-5793(89)81433-4.Peer-Reviewed Original Research
1988
Yeast RNase P: catalytic activity and substrate binding are separate functions.
Nichols M, Söll D, Willis I. Yeast RNase P: catalytic activity and substrate binding are separate functions. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 1379-1383. PMID: 3278310, PMCID: PMC279774, DOI: 10.1073/pnas.85.5.1379.Peer-Reviewed Original ResearchConceptsPrecursor tRNAsRNase PSubstrate bindingGel retardationCatalytic functionRibonucleoprotein RNase PDistinct sequence preferencesEnzyme catalytic functionRNase P cleavage siteMature tRNARNase P.Catalytic integrityTRNA precursorsRNA moietyRNA componentSequence preferenceTRNATRNA complexProtein componentsAcceptor stemEnzyme mechanismMaximal cleavageSecond nucleotideCleavage siteEnzyme
1986
Two RNA species co‐purify with RNase P from the fission yeast Schizosaccharomyces pombe.
Krupp G, Cherayil B, Frendewey D, Nishikawa S, Söll D. Two RNA species co‐purify with RNase P from the fission yeast Schizosaccharomyces pombe. The EMBO Journal 1986, 5: 1697-1703. PMID: 3743551, PMCID: PMC1166996, DOI: 10.1002/j.1460-2075.1986.tb04413.x.Peer-Reviewed Original ResearchConceptsM1 RNARNA speciesK RNASecondary structureFission yeast SchizosaccharomycesRNase P activityYeast genomic DNALimited sequence homologyYeast SchizosaccharomycesHaploid genomeSchizosaccharomyces pombeRNase PSingle copySouthern analysisSequence homologyGenomic DNAP activityRNAEscherichia coliHairpin loopSame basic organizationEnzyme activityBasic organizationInactivation experimentsSpecies
1982
Post-transcriptional nucleotide addition is responsible for the formation of the 5' terminus of histidine tRNA.
Cooley L, Appel B, Söll D. Post-transcriptional nucleotide addition is responsible for the formation of the 5' terminus of histidine tRNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1982, 79: 6475-6479. PMID: 6292903, PMCID: PMC347149, DOI: 10.1073/pnas.79.21.6475.Peer-Reviewed Original ResearchConceptsMature tRNAHistidine tRNAPrimary transcriptHistidine tRNA genesGuanylate residuePost-transcriptional additionDrosophila Kc cellsTRNA genesDrosophila melanogasterSchizosaccharomyces pombeTRNAs resultsRNA speciesRNase PEukaryotic mRNAsKc cellsRNA precursorsTRNASequence analysisNucleotide additionAdditional nucleotidesPhosphodiester bondGenesNucleotidesMaturation schemeTranscripts
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