1993
Identification of a 100‐kDa protein associated with nuclear ribonuclease P activity in Schizosaccharomyces pombe
ZIMMERLY S, DRAINAS D, SYLVERS L, Dieter S. Identification of a 100‐kDa protein associated with nuclear ribonuclease P activity in Schizosaccharomyces pombe. The FEBS Journal 1993, 217: 501-507. PMID: 8223594, DOI: 10.1111/j.1432-1033.1993.tb18270.x.Peer-Reviewed Original ResearchConceptsFission yeast Schizosaccharomyces pombeYeast Schizosaccharomyces pombeGlycerol gradient fractionationCross-linking experimentsPrecursor tRNAsSchizosaccharomyces pombeRibonuclease PProtein interactsRNA componentProtein componentsP activityRibonuclease P activityApparent homogeneityDEAE-cellulose chromatographyPhosphocellulose chromatographySpecific fashionProtein
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
Substrate 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
The unusually long amino acid acceptor stem of Escherichia coli selenocysteine tRNA results from abnormal cleavage by RNase P
Burkard U, Söll D. The unusually long amino acid acceptor stem of Escherichia coli selenocysteine tRNA results from abnormal cleavage by RNase P. Nucleic Acids Research 1988, 16: 11617-11624. PMID: 3062578, PMCID: PMC339093, DOI: 10.1093/nar/16.24.11617.Peer-Reviewed Original ResearchThe 5′-terminal guanylate of chloroplast histidine tRNA is encoded in its gene.
Burkard U, Söll D. The 5′-terminal guanylate of chloroplast histidine tRNA is encoded in its gene. Journal Of Biological Chemistry 1988, 263: 9578-9581. PMID: 2838471, DOI: 10.1016/s0021-9258(19)81555-7.Peer-Reviewed Original ResearchAnimalsBase SequenceChloroplastsCyanobacteriaDNA, RecombinantEndoribonucleasesEscherichia coliEscherichia coli ProteinsEuglena gracilisGuanine NucleotidesGuanosine MonophosphateMolecular Sequence DataPentosyltransferasesPlantsRibonuclease PRNA PrecursorsRNA, Transfer, Amino Acid-SpecificRNA, Transfer, HisSaccharomyces cerevisiaeVegetablesYeast 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 siteEnzymeProcessing of histidine transfer RNA precursors. Abnormal cleavage site for RNase P.
Burkard U, Willis I, Söll D. Processing of histidine transfer RNA precursors. Abnormal cleavage site for RNase P. Journal Of Biological Chemistry 1988, 263: 2447-2451. PMID: 3276688, DOI: 10.1016/s0021-9258(18)69227-0.Peer-Reviewed Original Research
1987
Substrate recognition and identification of splice sites by the tRNA-splicing endonuclease and ligase from Saccharomyces cerevisiae.
Greer C, Söll D, Willis I. Substrate recognition and identification of splice sites by the tRNA-splicing endonuclease and ligase from Saccharomyces cerevisiae. Molecular And Cellular Biology 1987, 7: 76-84. PMID: 3550427, PMCID: PMC365043, DOI: 10.1128/mcb.7.1.76.Peer-Reviewed Original Research
1986
Functional complementation between mutations in a yeast suppressor tRNA gene reveals potential for evolution of tRNA sequences.
Willis I, Nichols M, Chisholm V, Söll D, Heyer W, Szankasi P, Amstutz H, Munz P, Kohli J. Functional complementation between mutations in a yeast suppressor tRNA gene reveals potential for evolution of tRNA sequences. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 7860-7864. PMID: 3532123, PMCID: PMC386822, DOI: 10.1073/pnas.83.20.7860.Peer-Reviewed Original ResearchConceptsMutant tRNA precursorS. pombe genesSuppressor tRNA geneNucleotide sequence evolutionRNA processing levelRNase P cleavagePombe geneTRNA genesFunctional complementationComplementation eventsS. pombeCycle of inactivationTRNA sequencesTRNA precursorsSequence evolutionSaccharomyces cerevisiaeS. cerevisiaePombe strainSchizosaccharomyces pombe strainStructural domainsDifferential expressionSuppressor functionP cleavageGenesSuppressorTwo 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 experimentsSpeciesA single base change in the intron of a serine tRNA affects the rate of RNase P cleavage in vitro and suppressor activity in vivo in Saccharomyces cerevisiae.
Willis I, Frendewey D, Nichols M, Hottinger-Werlen A, Schaack J, Söll D. A single base change in the intron of a serine tRNA affects the rate of RNase P cleavage in vitro and suppressor activity in vivo in Saccharomyces cerevisiae. Journal Of Biological Chemistry 1986, 261: 5878-5885. PMID: 3516987, DOI: 10.1016/s0021-9258(17)38465-x.Peer-Reviewed Original ResearchThe additional guanylate at the 5' terminus of Escherichia coli tRNAHis is the result of unusual processing by RNase P.
Orellana O, Cooley L, Söll D. The additional guanylate at the 5' terminus of Escherichia coli tRNAHis is the result of unusual processing by RNase P. Molecular And Cellular Biology 1986, 6: 525-529. PMID: 3023854, PMCID: PMC367542, DOI: 10.1128/mcb.6.2.525.Peer-Reviewed Original Research