1997
Aminoacyl-tRNA synthesis: divergent routes to a common goal
Ibba M, Curnow A, Söll D. Aminoacyl-tRNA synthesis: divergent routes to a common goal. Trends In Biochemical Sciences 1997, 22: 39-42. PMID: 9048478, DOI: 10.1016/s0968-0004(96)20033-7.Peer-Reviewed Original ResearchConceptsTRNA-dependent transformationProtein-protein interactionsAminoacyl-tRNA synthesisProtein synthesisTRNAAdaptation mechanismsArchaeaKey componentDivergent routetRNA-dependent amino acid transformations.
Curnow A, Hong K, Yuan R, Söll D. tRNA-dependent amino acid transformations. Nucleic Acids Symposium Series 1997, 2-4. PMID: 9478189.Peer-Reviewed Original Research
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 proteinPurification and functional characterization of glutamate-1-semialdehyde aminotransferase from Chlamydomonas reinhardtii.
Jahn D, Chen M, Söll D. Purification and functional characterization of glutamate-1-semialdehyde aminotransferase from Chlamydomonas reinhardtii. Journal Of Biological Chemistry 1991, 266: 161-167. PMID: 1985889, DOI: 10.1016/s0021-9258(18)52416-9.Peer-Reviewed Original ResearchMeSH KeywordsAminooxyacetic AcidCell MembraneChlamydomonasChromatography, DEAE-CelluloseChromatography, GelChromatography, High Pressure LiquidChromatography, Ion ExchangeCyclohexanecarboxylic AcidsElectrophoresis, Polyacrylamide GelIntramolecular TransferasesIsomerasesKineticsMolecular WeightPyridoxal PhosphateConceptsGlutamate-1-semialdehyde aminotransferaseGlutamyl-tRNA synthetaseC5 pathwayChlamydomonas reinhardtiiGreen alga Chlamydomonas reinhardtiiGlu-tRNA reductaseTRNA-dependent transformationChloroplasts of plantsGlutamyl-tRNA reductaseAlga Chlamydomonas reinhardtiiDelta-aminolevulinic acidApparent molecular massWhole cell extractsChlorophyll biosynthesisSodium dodecyl sulfate-polyacrylamide gel electrophoresisC. reinhardtiiDodecyl sulfate-polyacrylamide gel electrophoresisSulfate-polyacrylamide gel electrophoresisRate zonal sedimentationFunctional characterizationThird enzymeGlycerol gradientsCell extractsReinhardtiiMembrane fraction
1990
Purification 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
1989
δ-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA
O'Neill G, Chen M, Söll D. δ-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA. FEMS Microbiology Letters 1989, 60: 255-259. DOI: 10.1111/j.1574-6968.1989.tb03482.x.Peer-Reviewed Original ResearchΔ‐Aminolevulinic acid biosynthesisChloroplasts of algaeTRNA-dependent transformationB. subtilisE. coliBacillus subtilisHigher plant speciesEscherichia coliPlant speciesAnaerobic eubacteriaAcid biosynthesisCell-free extractsCell extractsΔ-aminolevulinic acidBiosynthetic activitySubtilisColiGabaculinAbstract Cell-free extractsAnaerobic conditionsAlaEubacteriaArchaebacteriaChloroplastsCyanobacteriadelta-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA.
O'Neill G, Chen M, Söll D. delta-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA. FEMS Microbiology Letters 1989, 51: 255-9. PMID: 2511063, DOI: 10.1016/0378-1097(89)90406-0.Peer-Reviewed Original ResearchConceptsDelta-aminolevulinic acid biosynthesisChloroplasts of algaeTRNA-dependent transformationB. subtilisE. coliBacillus subtilisHigher plant speciesEscherichia coliPlant speciesAnaerobic eubacteriaGlutamyl-tRNAAcid biosynthesisCell-free extractsCell extractsBiosynthetic activitySubtilisDelta-aminolevulinic acidColiGabaculinAnaerobic conditionsAlaEubacteriaArchaebacteriaChloroplastsCyanobacteria