1994
Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis.
Ilag L, Kumar A, Söll D. Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis. The Plant Cell 1994, 6: 265-275. PMID: 7908550, PMCID: PMC160432, DOI: 10.1105/tpc.6.2.265.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde OxidoreductasesAmino Acid SequenceAminolevulinic AcidArabidopsisChlorophyllChloroplastsEscherichia coliGene Expression RegulationGenes, PlantGlutamatesGlutamic AcidIntramolecular TransferasesIsomerasesLightMolecular Sequence DataPromoter Regions, GeneticRNA, Transfer, GluSequence Homology, Amino AcidSequence Homology, Nucleic AcidTranscription, GeneticConceptsC5 pathwayAmino acid sequenceHemA proteinChlorophyll biosynthesisGlu-tRNAALA formationAcid sequenceRNA gel blot analysisDeduced amino acid sequenceGlu-tRNA reductaseChloroplasts of plantsGel blot analysisArabidopsis genesFunctional complementationShort intronsCorresponding genesTranscriptional controlFlower tissuesLight regulationExtensive homologyFirst enzymeUniversal precursorReductase geneChlorophyll formationSecond enzyme
1991
Two glutamyl-tRNA reductase activities in Escherichia coli
Jahn D, Michelsen U, Söll D. Two glutamyl-tRNA reductase activities in Escherichia coli. Journal Of Biological Chemistry 1991, 266: 2542-2548. PMID: 1990004, DOI: 10.1016/s0021-9258(18)52279-1.Peer-Reviewed Original ResearchConceptsReductase activityGlu-tRNA reductaseMolecular massEscherichia coliApparent molecular massDifferent chromatographic separationsSequence-specific recognitionGlycerol gradient centrifugationThree-step conversionTetrapyrrole biosynthesisChlamydomonas reinhardtiiE. coli K12ALA formationChromatographic separationKey enzymeMonomeric structureActive enzymeBacillus subtilisColi K12Nondenaturing conditionsHomogeneous proteinMolecular weightDelta-aminolevulinic acidEnzyme activityAddition of GTP
1990
Purification and functional characterization of the Glu-tRNA(Gln) amidotransferase from Chlamydomonas reinhardtii.
Jahn D, Kim Y, Ishino Y, Chen M, Söll D. Purification and functional characterization of the Glu-tRNA(Gln) amidotransferase from Chlamydomonas reinhardtii. Journal Of Biological Chemistry 1990, 265: 8059-8064. PMID: 1970821, DOI: 10.1016/s0021-9258(19)39038-6.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmmoniaAsparagineAzo CompoundsBinding SitesChlamydomonasElectrophoresis, Polyacrylamide GelEnzyme ActivationGlutamatesGlutamic AcidGlutamineMagnesiumMolecular WeightNitrogenous Group TransferasesNorleucinePhosphorylationProtein DenaturationRNA, Transfer, Amino AcylSpectrophotometrySubstrate SpecificityTransferasesConceptsChlamydomonas reinhardtiiGlutamyl-tRNA synthetaseGlycerol gradient sedimentationSodium dodecyl sulfate-polyacrylamide gelsDodecyl sulfate-polyacrylamide gelsAmide donorSulfate-polyacrylamide gelsGlutamine-dependent reactionGlutamine amidotransferasesPresence of ATPGreen algaeSpecific amidotransferaseFunctional characterizationGlutaminyl-tRNAAmidotransferaseLow glutaminase activityApparent MrGradient sedimentationAlpha 2 structureReinhardtiiEnzymeATPGlutaminase activityStable complexesAmmonia-dependent reaction
1988
Formation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species
O'Neill G, Peterson D, Schön A, Chen M, Söll D. Formation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species. Journal Of Bacteriology 1988, 170: 3810-3816. PMID: 2900830, PMCID: PMC211375, DOI: 10.1128/jb.170.9.3810-3816.1988.Peer-Reviewed Original ResearchConceptsPrecursor delta-aminolevulinic acidHigher plantsUnicellular cyanobacterium Synechocystis spGlutamate-1-semialdehyde aminotransferaseCell extractsCyanobacterium Synechocystis spDelta-aminolevulinic acidSouthern blot analysisIdentical primary sequencesSynechocystis spNucleotide modificationsConversion of glutamateGene copiesALA synthesisPrimary sequenceSequence specificityTerminal enzymePolyacrylamide gel electrophoresisChloroplastsEuglena gracilisEscherichia coliSpeciesBlot analysisTRNAGel electrophoresisMisaminoacylation and transamidation are required for protein biosynthesis in lactobacillus bulgaricus
Schön A, Hottinger H, Söll D. Misaminoacylation and transamidation are required for protein biosynthesis in lactobacillus bulgaricus. Biochimie 1988, 70: 391-394. PMID: 3139057, DOI: 10.1016/0300-9084(88)90212-x.Peer-Reviewed Original Research
1979
The nucleotide sequence of the major glutamate transfer RNA from Schizosaccharomyces pombe
Wong T, McCutchan T, Kohli J, Söll D. The nucleotide sequence of the major glutamate transfer RNA from Schizosaccharomyces pombe. Nucleic Acids Research 1979, 6: 2057-2068. PMID: 379816, PMCID: PMC327836, DOI: 10.1093/nar/6.6.2057.Peer-Reviewed Original Research
1976
Studies of the complex between transfer RNAs with complementary anticodons I. Origins of enhanced affinity between complementary triplets
Grosjean H, Söll D, Crothers D. Studies of the complex between transfer RNAs with complementary anticodons I. Origins of enhanced affinity between complementary triplets. Journal Of Molecular Biology 1976, 103: 499-519. PMID: 781277, DOI: 10.1016/0022-2836(76)90214-x.Peer-Reviewed Original Research
1975
A method for the isolation of specific tRNA precursors.
Vögeli G, Grosjean H, Söll D. A method for the isolation of specific tRNA precursors. Proceedings Of The National Academy Of Sciences Of The United States Of America 1975, 72: 4790-4794. PMID: 1108001, PMCID: PMC388817, DOI: 10.1073/pnas.72.12.4790.Peer-Reviewed Original ResearchStudies of the complex between transfer RNA molecules and complementary anticodons: kinetic and thermodynamic aspects.
Grosjean H, Söll D, Crothers D. Studies of the complex between transfer RNA molecules and complementary anticodons: kinetic and thermodynamic aspects. Archives Of Physiology And Biochemistry 1975, 83: 970-1. PMID: 58627.Peer-Reviewed Original Research
1974
Nuclear magnetic resonance studies of protein-nucleic acid interactions II. The E. coli tRNAGlu complex with glutamyl-tRNA synthetase
Shulman R, Hilbers C, Söll D, Yang S. Nuclear magnetic resonance studies of protein-nucleic acid interactions II. The E. coli tRNAGlu complex with glutamyl-tRNA synthetase. Journal Of Molecular Biology 1974, 90: 609-611. PMID: 4615173, DOI: 10.1016/0022-2836(74)90238-1.Peer-Reviewed Original ResearchCovalent attachment of fluorescent groups to transfer ribonucleic acid. Reactions with 4-bromomethyl-7-methoxy-2-oxo-2H-benzopyran.
Yang C, Soell D. Covalent attachment of fluorescent groups to transfer ribonucleic acid. Reactions with 4-bromomethyl-7-methoxy-2-oxo-2H-benzopyran. Biochemistry 1974, 13: 3615-21. PMID: 4367729, DOI: 10.1021/bi00714a033.Peer-Reviewed Original ResearchAlkaline PhosphataseAmino Acyl-tRNA SynthetasesBenzopyransBromineCarbon RadioisotopesEscherichia coliFluorescenceFormatesGlutamatesMethionineMethyl EthersModels, ChemicalNucleosidesPhosphoric Diester HydrolasesPseudouridineRibonucleasesRNA, BacterialRNA, TransferSpectrometry, FluorescenceStructure-Activity RelationshipTransfer RNA AminoacylationUridineInvolvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation
Seno T, Agris P, Söll D. Involvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation. Biochimica Et Biophysica Acta 1974, 349: 328-338. PMID: 4366808, DOI: 10.1016/0005-2787(74)90120-8.Peer-Reviewed Original ResearchAdenosine TriphosphateAmino Acyl-tRNA SynthetasesCarbon RadioisotopesChromatography, Ion ExchangeCyanogen BromideDiphosphatesEscherichia coliGlutamatesGlutamineKineticsPhosphorus RadioisotopesProtein BiosynthesisRNA, BacterialRNA, TransferSpectrophotometry, UltravioletThiouridineTransfer RNA Aminoacylation
1973
Biological function of 2-thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid.
Agris P, Soell D, Seno T. Biological function of 2-thiouridine in Escherichia coli glutamic acid transfer ribonucleic acid. Biochemistry 1973, 12: 4331-7. PMID: 4584321, DOI: 10.1021/bi00746a005.Peer-Reviewed Original ResearchAmino Acyl-tRNA SynthetasesCarbon RadioisotopesChromatography, Ion ExchangeChromatography, Thin LayerCyanogen BromideElectrophoresis, DiscElectrophoresis, Polyacrylamide GelEscherichia coliGlutamatesKineticsMutationProtein BiosynthesisRNA, BacterialRNA, TransferSpectrophotometry, UltravioletSulfurSulfur RadioisotopesThiouridineTritium
1972
Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli I. PURIFICATION AND PROPERTIES
Lapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli I. PURIFICATION AND PROPERTIES. Journal Of Biological Chemistry 1972, 247: 4966-4974. PMID: 4341531, DOI: 10.1016/s0021-9258(19)44925-9.Peer-Reviewed Original ResearchAdenosine TriphosphateAlkylationAmino AcidsAmino Acyl-tRNA SynthetasesAnimalsCatalysisCentrifugation, ZonalChromatographyDiphosphatesDrug StabilityElectrophoresisElectrophoresis, DiscEscherichia coliGlutamatesHot TemperatureHydroxyapatitesIsoelectric FocusingMacromolecular SubstancesMolecular WeightOxidation-ReductionPhosphorus IsotopesRabbitsUltracentrifugationGlutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID
Lapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID. Journal Of Biological Chemistry 1972, 247: 4975-4981. PMID: 4341532, DOI: 10.1016/s0021-9258(19)44926-0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acyl-tRNA SynthetasesCarbon IsotopesCatalysisCentrifugation, Density GradientDiphosphatesDrug StabilityEscherichia coliGlutamatesHot TemperatureHydrogen-Ion ConcentrationKineticsLeucineMagnesiumPhosphorus IsotopesProtein BindingRNA, TransferSpectrometry, FluorescenceValineConceptsGlutamyl-transfer ribonucleic acid synthetaseEscherichia coli IITransfer ribonucleic acidTRNA-GluTRNA-ValTRNA-LeuCognate tRNABiological specificityRibonucleic acidPure enzymeEnzymeSimilar Km valuesComplex formationGradient centrifugationSynthetaseKm valuesFluorescence-quenching studiesTRNAIsoacceptorsComplexesFluorescence quenching studiesHeat inactivationInactivationLeuGluGlutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli III. INFLUENCE OF THE 46K PROTEIN ON THE AFFINITY OF THE 56K GLUTAMYL TRANSFER RIBONUCLEIC ACID SYNTHETASE FOR ITS SUBSTRATES
Lapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli III. INFLUENCE OF THE 46K PROTEIN ON THE AFFINITY OF THE 56K GLUTAMYL TRANSFER RIBONUCLEIC ACID SYNTHETASE FOR ITS SUBSTRATES. Journal Of Biological Chemistry 1972, 247: 4982-4985. PMID: 4560497, DOI: 10.1016/s0021-9258(19)44927-2.Peer-Reviewed Original Research