1997
Glutaminyl-tRNA synthetase.
Freist W, Gauss D, Ibba M, Söll D. Glutaminyl-tRNA synthetase. Biological Chemistry 1997, 378: 1103-17. PMID: 9372179.Peer-Reviewed Original ResearchConceptsE. coli GlnRSGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseMammalian enzymeCommon ancestorPositive eubacteriaCognate tRNAMultienzyme complexTRNA moleculesGlnRArtificial mutantsAcceptor stemAnticodon loopMolecular massAmino acidsCatalytic siteEnzymeSynthetaseEubacteriaArchaebacteriaTRNAMutantsOrganellesAncestorComplexes
1991
The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase
Ilag L, Jahn D, Eggertsson G, Söll D. The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase. Journal Of Bacteriology 1991, 173: 3408-3413. PMID: 2045363, PMCID: PMC207952, DOI: 10.1128/jb.173.11.3408-3413.1991.Peer-Reviewed Original ResearchMeSH KeywordsAminolevulinic AcidCentrifugation, Density GradientChromatography, High Pressure LiquidCloning, MolecularDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEscherichia coliIntramolecular TransferasesIsomerasesMolecular WeightPyridoxal PhosphatePyridoxamineTransformation, GeneticConceptsGlu-tRNA reductaseTRNA-dependent transformationApparent native molecular massMolecular massGlutamyl-tRNA synthetaseNative molecular massAminoglycoside antibiotic kanamycinHemL geneWild-type DNAAuxotrophic phenotypeC5 pathwaySodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisMap positionGSA aminotransferasePhysical mappingSulfate-polyacrylamide gel electrophoresisRate zonal sedimentationGene productsThird enzymeGlycerol gradientsApparent homogeneityAntibiotic kanamycinEscherichia coliPure proteinTwo 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 characterization of Chlamydomonas reinhardtii chloroplast glutamyl-tRNA synthetase, a natural misacylating enzyme.
Chen M, Jahn D, Schön A, O'Neill G, Söll D. Purification and characterization of Chlamydomonas reinhardtii chloroplast glutamyl-tRNA synthetase, a natural misacylating enzyme. Journal Of Biological Chemistry 1990, 265: 4054-4057. PMID: 2303494, DOI: 10.1016/s0021-9258(19)39701-7.Peer-Reviewed Original ResearchConceptsGlutamyl-tRNA synthetaseChloroplast enzymeApparent molecular massSequential column chromatographyChlamydomonas reinhardtiiActive enzymeMolecular massNondenaturing conditionsEscherichia coliDenaturing conditionsAcceptor RNASynthetaseMono S.Mono QEnzymeTRNAReinhardtiiYeastColumn chromatographyRNACytoplasmicProteinBarleyColiReversed phase chromatographyPurification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis.
Chen M, Jahn D, O'Neill G, Söll D. Purification of the glutamyl-tRNA reductase from Chlamydomonas reinhardtii involved in delta-aminolevulinic acid formation during chlorophyll biosynthesis. Journal Of Biological Chemistry 1990, 265: 4058-4063. PMID: 2303495, DOI: 10.1016/s0021-9258(19)39702-9.Peer-Reviewed Original ResearchConceptsGlu-tRNA reductaseGlutamyl-tRNA reductaseGlu-tRNAChlamydomonas reinhardtiiTRNA-dependent transformationChloroplasts of plantsDelta-aminolevulinic acid formationApparent molecular massChlorophyll biosynthesisGlutamyl-tRNAHomologous tRNAsSecond enzymeActive enzymeMolecular massNondenaturing conditionsDifferent chromatographic separationsCertain bacteriaReductaseDelta-aminolevulinic acidReinhardtiiPorphyrin biosynthesisBiosynthesisStable complexesChromatographic separationCarboxyl groups
1986
The RNA required in the first step of chlorophyll biosynthesis is a chloroplast glutamate tRNA
Schön A, Krupp G, Gough S, Berry-Lowe S, Kannangara C, Söll D. The RNA required in the first step of chlorophyll biosynthesis is a chloroplast glutamate tRNA. Nature 1986, 322: 281-284. PMID: 3637637, DOI: 10.1038/322281a0.Peer-Reviewed Original ResearchConceptsΔ-aminolevulinatePeptide bond synthesisCognate amino acidMolecules of chlorophyllLow relative molecular massNucleotide sequence analysisRelative molecular massBond synthesisSubsequent reactionChlorophyll biosynthesisTransfer RNAUniversal precursorGlutamate tRNAAminoacyl bondSequence analysisNovel roleSerial affinity chromatographyMolecular massRNAAmino acidsComplete reactionBlue SepharoseAcceptor RNAReduction of glutamateReaction