2000
Cysteine Biosynthesis Pathway in the ArchaeonMethanosarcina barkeri Encoded by Acquired Bacterial Genes?
Kitabatake M, So M, Tumbula D, Söll D. Cysteine Biosynthesis Pathway in the ArchaeonMethanosarcina barkeri Encoded by Acquired Bacterial Genes? Journal Of Bacteriology 2000, 182: 143-145. PMID: 10613873, PMCID: PMC94250, DOI: 10.1128/jb.182.1.143-145.2000.Peer-Reviewed Original ResearchConceptsCysteine biosynthesis pathwayCysK geneCysteine biosynthesisBiosynthesis pathwayRecent genome dataOpen reading framePyrococcus sppCysE geneBacterial genesMethanococcus jannaschiiGenome dataArchaeoglobus fulgidusReading frameSulfolobus solfataricusThermoplasma acidophilumCysM geneMethanobacterium thermoautotrophicumGenesBiosynthesisPathwayGreat similaritySame functionCysKOrthologsArchaea
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 cerevisiaeVegetablesProcessing 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
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 experimentsSpeciesThe 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
1981
Partial purification of RNase P from Schizosaccharomyces pombe.
Kline L, Nishikawa S, Söll D. Partial purification of RNase P from Schizosaccharomyces pombe. Journal Of Biological Chemistry 1981, 256: 5058-5063. PMID: 6262315, DOI: 10.1016/s0021-9258(19)69366-x.Peer-Reviewed Original ResearchMeSH KeywordsAscomycotaBase SequenceEndonucleasesEscherichia coli ProteinsKineticsMicrococcal NucleaseRibonuclease PRibonucleasesRNA, TransferSchizosaccharomycesSubstrate SpecificityConceptsSimple assay procedureNucleic acid componentsColumn chromatographyReaction productsEnzyme purificationPhosphocellulose column chromatographyAcid componentsSynthetic substratesAssay procedurePurificationAcid solubilityPartial purificationSubstrateYeast RNase PSolubilityChromatographyProductsSeparationPhosphateTrichloroacetic acid solubility