2014
Exploring the Substrate Range of Wild‐Type Aminoacyl‐tRNA Synthetases
Fan C, Ho JM, Chirathivat N, Söll D, Wang Y. Exploring the Substrate Range of Wild‐Type Aminoacyl‐tRNA Synthetases. ChemBioChem 2014, 15: 1805-1809. PMID: 24890918, PMCID: PMC4133344, DOI: 10.1002/cbic.201402083.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetasesSubstrate rangeDifferent amino acid sitesAmino acidsE. coli tryptophanyl-tRNA synthetaseE. coli aminoacyl-tRNA synthetasesAmino acid sitesCanonical amino acidsNonstandard amino acidsTyrosyl-tRNA synthetaseTryptophanyl-tRNA synthetaseAnticodon sequenceTRNA synthetasesSynthetasesSynthetaseSequenceAnticodonNSAAsTrpRSProteinAminoacylAcid
2004
Cys-tRNACys formation and cysteine biosynthesis in methanogenic archaea: two faces of the same problem?
Ambrogelly A, Kamtekar S, Sauerwald A, Ruan B, Tumbula-Hansen D, Kennedy D, Ahel I, Söll D. Cys-tRNACys formation and cysteine biosynthesis in methanogenic archaea: two faces of the same problem? Cellular And Molecular Life Sciences 2004, 61: 2437-2445. PMID: 15526152, DOI: 10.1007/s00018-004-4194-9.Peer-Reviewed Original ResearchConceptsMethanogenic archaeaCysteine biosynthesisCellular translation machineryAminoacyl-tRNA synthesisCanonical cysteinyl-tRNA synthetaseAminoacyl-tRNA synthetasesCysteinyl-tRNA synthetaseRecognizable genesTranslation machineryGenome sequenceArchaeaBiosynthesisEssential componentSynthetasesTRNARibosomesGenesMachineryOrganismsSynthetasePossible linkSequenceFormation
2000
One Polypeptide with Two Aminoacyl-tRNA Synthetase Activities
Stathopoulos C, Li T, Longman R, Vothknecht U, Becker H, Ibba M, Söll D. One Polypeptide with Two Aminoacyl-tRNA Synthetase Activities. Science 2000, 287: 479-482. PMID: 10642548, DOI: 10.1126/science.287.5452.479.Peer-Reviewed Original ResearchConceptsProlyl-tRNA synthetaseProtein synthesisCysteinyl-tRNA synthetase activityAmino-terminal sequenceSynthetase activityAminoacyl-tRNA synthetase activityCertain archaeaEvolutionary originMethanococcus jannaschiiGenome sequenceSubstrate specificityGenetic analysisSuch organismsMessenger RNARNA synthetasesSynthetaseSequenceArchaeaJannaschiiSynthetasesRNAOrganismsPolypeptideProlylProtein
1994
Transfer RNA in Its Fourth Decade
RajBhandary U, Söll D. Transfer RNA in Its Fourth Decade. 1994, 1-4. DOI: 10.1128/9781555818333.ch1.Peer-Reviewed Original Research
1992
Chloroplast tRNAAsp: nucleotide sequence and variation of in vivo levels during plastid maturation
Schön A, Gough S, Söll D. Chloroplast tRNAAsp: nucleotide sequence and variation of in vivo levels during plastid maturation. Plant Molecular Biology 1992, 20: 601-607. PMID: 1450377, DOI: 10.1007/bf00046445.Peer-Reviewed Original Research
1991
The Human Genome Project: a paradigm for information management in the life sciences
Pearson M, Söll D. The Human Genome Project: a paradigm for information management in the life sciences. The FASEB Journal 1991, 5: 35-39. PMID: 1991581, DOI: 10.1096/fasebj.5.1.1991581.Peer-Reviewed Original Research
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
The selenocysteine-inserting opal suppressor serine tRNA from E.coli is highly unusual in structure and modification
Schön A, Böck A, Ott G, Sprinzl M, Söll D. The selenocysteine-inserting opal suppressor serine tRNA from E.coli is highly unusual in structure and modification. Nucleic Acids Research 1989, 17: 7159-7165. PMID: 2529478, PMCID: PMC334795, DOI: 10.1093/nar/17.18.7159.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesBase SequenceChromatography, High Pressure LiquidCodonCysteineEscherichia coliGenes, BacterialMolecular Sequence DataNucleic Acid ConformationRNA, Transfer, Amino Acid-SpecificRNA, Transfer, SerSeleniumSelenocysteineStructure-Activity RelationshipSuppression, Genetic
1986
The nucleotide sequence, localization and transcriptional properties of a tRNACUGLeu gene from Drosophila melanogaster
Glew L, Lo R, Recce T, Nichols M, Söll D, Bell J. The nucleotide sequence, localization and transcriptional properties of a tRNACUGLeu gene from Drosophila melanogaster. Gene 1986, 44: 307-314. PMID: 2946625, DOI: 10.1016/0378-1119(86)90195-2.Peer-Reviewed Original ResearchThe nucleotide sequence of a wheat γ-gliadin genomic clone
Sugiyama T, Rafalski A, Söll D. The nucleotide sequence of a wheat γ-gliadin genomic clone. Plant Science 1986, 44: 205-209. DOI: 10.1016/0168-9452(86)90092-0.Peer-Reviewed Original Research
1985
Dimeric tRNA gene arrangement in Schizosaccharomyces pombe allows increased expression of the downstream gene
Hottinger-Werlen A, Schaack J, Lapointe J, Mao J, Nichols M, Söll D. Dimeric tRNA gene arrangement in Schizosaccharomyces pombe allows increased expression of the downstream gene. Nucleic Acids Research 1985, 13: 8739-8747. PMID: 3936021, PMCID: PMC318948, DOI: 10.1093/nar/13.24.8739.Peer-Reviewed Original ResearchConceptsTRNASer geneS. pombe genesDimeric arrangementPombe geneTRNA genesGene arrangementSchizosaccharomyces pombeSpecies genesMinor genesTranscription factorsDownstream genesTranscriptional efficiencyCompetitive abilityGenesMinor speciesMajor speciesSpeciesDimeric structureEfficient productionExpressionSchizosaccharomycesPombeTRNASerSaccharomycesSequencesupN ochre suppressor gene in Escherichia coli codes for tRNALys
Uemura H, Thorbjarnardóttir S, Gamulin V, Yano J, Andrésson O, Söll D, Eggertsson G. supN ochre suppressor gene in Escherichia coli codes for tRNALys. Journal Of Bacteriology 1985, 163: 1288-1289. PMID: 3897192, PMCID: PMC219277, DOI: 10.1128/jb.163.3.1288-1289.1985.Peer-Reviewed Original ResearchNucleotide sequences of two serine tRNAs with a GGA anticodon: the structure-function relationships in the serine family of E. coli tRNAs
Grosjean H, Nicoghosian K, Haumont E, Söll D, Cedergren R. Nucleotide sequences of two serine tRNAs with a GGA anticodon: the structure-function relationships in the serine family of E. coli tRNAs. Nucleic Acids Research 1985, 13: 5697-5706. PMID: 3898020, PMCID: PMC321899, DOI: 10.1093/nar/13.15.5697.Peer-Reviewed Original ResearchConceptsSerine tRNANucleotide sequenceRecent common ancestorE. coli tRNACodon-anticodon interactionStructure-function relationshipsEubacterial originUCU codonsEvolutionary analysisCommon ancestorD-loopTRNAAnticodon stemSerine familyAnticodonGenesE. coliMinor speciesCodonMajor speciesSpeciesSequenceTRNASerAncestorSerineLeucine tRNA family of Escherichia coli: nucleotide sequence of the supP(Am) suppressor gene
Thorbjarnardóttir S, Dingermann T, Rafnar T, Andrésson O, Söll D, Eggertsson G. Leucine tRNA family of Escherichia coli: nucleotide sequence of the supP(Am) suppressor gene. Journal Of Bacteriology 1985, 161: 219-222. PMID: 2981802, PMCID: PMC214859, DOI: 10.1128/jb.161.1.219-222.1985.Peer-Reviewed Original ResearchConceptsSuppressor allelesLeuX geneAmber suppressor allelesMature coding sequenceLeucyl-tRNA synthetaseSingle base changeTRNA familiesCAA anticodonBox sequenceTermination signalDNA sequencesNucleotide sequenceBacteriophage T4Coding sequenceAminoacyl stemSuppressor geneLoop regionTRNABase changesEscherichia coliGenesE. coliSequenceColiAllelesEscherichia coli supH suppressor: temperature-sensitive missense suppression caused by an anticodon change in tRNASer2
Thorbjarnardóttir S, Uemura H, Dingermann T, Rafnar T, Thorsteinsdóttir S, Söll D, Eggertsson G. Escherichia coli supH suppressor: temperature-sensitive missense suppression caused by an anticodon change in tRNASer2. Journal Of Bacteriology 1985, 161: 207-211. PMID: 3155715, PMCID: PMC214857, DOI: 10.1128/jb.161.1.207-211.1985.Peer-Reviewed Original ResearchConceptsWild-type tRNASingle nucleotide changeWild-type sequenceCAA anticodonMissense suppressorMissense suppressionCUA anticodonDNA sequencesLeucine codonMutant formsInsertion of serineNucleotide changesSuppressor geneAnticodonTRNASupHTRNASer2Anticodon changeCodonSuppressorSequenceTRNASerCloningGenesSerine
1984
Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes.
Hoben P, Uemura H, Yamao F, Cheung A, Swanson R, Sumner-Smith M, Söll D. Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes. The FASEB Journal 1984, 43: 2972-6. PMID: 6389180.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseMutant enzymesWild-type GlnRSAmino-terminal halfAmino acid sequenceAmino acid changesStructural gene mutationsTranslational controlTRNA speciesRelaxed specificityGene sequencesAcid sequenceGlnRRegulation mechanismAcid changesMonomeric polypeptideAmino acidsEnzymeTRNATyrSynthetaseMutationsGene mutationsGlutamineSequenceMisaminoacylationThe sup8 tRNALeu gene of Schizosaccharomyces pombe has an unusual intervening sequence and reduced pairing in the anticodon stem
Sumner-Smith M, Hottinger H, Willis I, Koch T, Arentzen R, Söll D. The sup8 tRNALeu gene of Schizosaccharomyces pombe has an unusual intervening sequence and reduced pairing in the anticodon stem. Molecular Genetics And Genomics 1984, 197: 447-452. PMID: 6597338, DOI: 10.1007/bf00329941.Peer-Reviewed Original ResearchConceptsTRNA genesS. pombe DNAWild-type alleleAnticodon UCASplicing endonucleaseSuppressor allelesSchizosaccharomyces pombeTRNALeu geneUUA codonTrailer sequencesIntervening sequenceCell-free extractsAnticodon stemRelated sequencesSplice siteBase pairsSecondary structureGenesIsoacceptorsAllelesSequenceStructural requirementsPombeAnticodonSup8Mutations affecting excision of the intron from a eukaryotic dimeric tRNA precursor.
Willis I, Hottinger H, Pearson D, Chisholm V, Leupold U, Söll D. Mutations affecting excision of the intron from a eukaryotic dimeric tRNA precursor. The EMBO Journal 1984, 3: 1573-1580. PMID: 6430697, PMCID: PMC557561, DOI: 10.1002/j.1460-2075.1984.tb02013.x.Peer-Reviewed Original ResearchConceptsTRNA precursorsDimeric tRNA precursorSerine tRNA geneEfficiency of splicingPrecursor tRNA processingSingle base changeTRNA genesTRNASer geneTRNA processingGene transcriptionNucleotide sequenceUGA mutationsD-loopMutant geneGenesBase changesExtra armMutationsIntronsTranscriptionVivo systemDimeric precursorSequenceTRNASerSplicingThe extent of a eukaryotic tRNA gene. 5‘- and 3‘-flanking sequence dependence for transcription and stable complex formation.
Schaack J, Sharp S, Dingermann T, Burke DJ, Cooley L, Söll D. The extent of a eukaryotic tRNA gene. 5‘- and 3‘-flanking sequence dependence for transcription and stable complex formation. Journal Of Biological Chemistry 1984, 259: 1461-1467. PMID: 6693417, DOI: 10.1016/s0021-9258(17)43429-6.Peer-Reviewed Original ResearchConceptsStable complex formationBase pairsDrosophila Kc cell extractSequence requirementsCell extractsEukaryotic tRNA genesStable transcription complexesHeLa cell extractsTRNA genesComplex formationTranscription complexArg genesEfficient transcriptionTranscription assaysTranscription propertiesCell-free extractsTranscriptionHomologous systemGenesSequenceSequence dependenceCellular sourceExtractAssaysPairs
1983
Six Schizosaccharomyces pombe tRNA genes including a gene for a tRNA Lys with an intervening sequence which cannot base-pair with the anticodon
Gamulin V, Mao J, Appel B, Sumner-Smith M, Yamao F, Söll D. Six Schizosaccharomyces pombe tRNA genes including a gene for a tRNA Lys with an intervening sequence which cannot base-pair with the anticodon. Nucleic Acids Research 1983, 11: 8537-8546. PMID: 6561518, PMCID: PMC326605, DOI: 10.1093/nar/11.24.8537.Peer-Reviewed Original Research