1999
Selective inhibition of HEMA gene expression by photooxidation in Arabidopsis thaliana
Kumar M, Chaturvedi S, Söll D. Selective inhibition of HEMA gene expression by photooxidation in Arabidopsis thaliana. Phytochemistry 1999, 51: 847-851. PMID: 10423858, DOI: 10.1016/s0031-9422(99)00114-4.Peer-Reviewed Original ResearchConceptsArabidopsis thalianaChloroplasts of plantsGlutamyl-tRNA reductaseCarotenoid biosynthesisFirst enzymeALA formationPhotobleaching herbicidesPhotooxidative damageGene expressionSelective inhibitionCarotenoid pigmentsNorflurazonThalianaPlantsChloroplastsFirst precursorPathwayExpressionEnzymeInitial metaboliteAlaBiosynthesisInhibitionTetrapyrrolesGlutamate
1996
A second and differentially expressed glutamyl-tRNA reductase gene from Arabidopsis thaliana
Kumar A, Csankovszki G, Söll D. A second and differentially expressed glutamyl-tRNA reductase gene from Arabidopsis thaliana. Plant Molecular Biology 1996, 30: 419-426. PMID: 8605295, DOI: 10.1007/bf00049321.Peer-Reviewed Original ResearchConceptsAbstract5-Aminolevulinic acidHemA geneArabidopsis thalianaC5 pathwayGlutamyl-tRNA reductase geneDeduced amino acid sequenceLight-inducible genesChloroplasts of plantsGlutamyl-tRNA reductaseAmino acid sequenceA. thalianaChlorophyll biosynthesisShort intronsGenomic libraryGlutamyl-tRNARegulatory elementsALA formationNucleotide sequenceUniversal precursorAcid sequenceReductase geneGenomic DNAThalianaGenesAmino acids
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
1993
Incomplete citric acid cycle obliges aminolevulinic acid synthesis via the C5 pathway in a methylotroph
Lloyd A, Weitzman P, Söll D. Incomplete citric acid cycle obliges aminolevulinic acid synthesis via the C5 pathway in a methylotroph. Microbiology 1993, 139: 2931-2938. DOI: 10.1099/00221287-139-12-2931.Peer-Reviewed Original ResearchC5 pathwayM. methylotrophusAminolevulinic acid synthesisTRNA-dependent mannerConversion of pyruvateCitric acid cycleMalate dehydrogenase activityMammalian cellsGlyoxylate cycleALA formationCell-free extractsGlu-tRNAGluAcid cycleIsocitrate dehydrogenaseMethylophilus methylotrophusCatabolic roleAcid synthesisPathwayEnzymic activityDehydrogenase activityEnzymeConnected pathwaysAlaMethylotrophsYeast
1992
Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression.
Verkamp E, Jahn M, Jahn D, Kumar A, Söll D. Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression. Journal Of Biological Chemistry 1992, 267: 8275-8280. PMID: 1569081, DOI: 10.1016/s0021-9258(18)42438-6.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde OxidoreductasesAmino Acid SequenceBase SequenceChromatography, GelCyanobacteriaEscherichia coliGene ExpressionGenes, BacterialGenes, FungalGenetic Complementation TestMolecular Sequence DataOpen Reading FramesPlasmidsRestriction MappingSaccharomyces cerevisiaeSequence Homology, Nucleic AcidConceptsGlutamyl-tRNA reductaseHemA geneAmino acid sequenceHemA proteinGluTR activitySynechocystis 6803Acid sequenceE. coliGlutamate-1-semialdehyde aminotransferaseHemA gene productEscherichia coliCyanobacterium Synechocystis spOpen reading frameEnterobacterium Escherichia coliDNA sequence analysisFunctional complementationGene structureGlu-tRNAGel filtration experimentsPCC 6803Synechocystis spGlutamyl-tRNAAcid polypeptideReading frameALA formation
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 GTPdelta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli
O'Neill G, Thorbjarnardóttir S, Michelsen U, Pálsson S, Söll D, Eggertsson G. delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli. Journal Of Bacteriology 1991, 173: 94-100. PMID: 1987138, PMCID: PMC207161, DOI: 10.1128/jb.173.1.94-100.1991.Peer-Reviewed Original ResearchConceptsALA dehydratase activityEscherichia coliWild-type geneClasses of mutantsDNA sequence analysisAminoglycoside antibiotic kanamycinHeme biosynthetic pathwayALA biosynthesisWild-type DNAAuxotrophic phenotypeComplementation studiesDehydratase activityHemB geneBiosynthetic pathwayPositive regulationALA formationSame geneMutantsPenicillin enrichmentSequence analysisGenesAntibiotic kanamycinDiffusible productHemB mutantEnzymatic activity
1988
The nucleotide sequences of barley cytoplasmic glutamate transfer RNAs and structural features essential for formation of δ-aminolevulinic acid
Peterson D, Schön A, Söll D. The nucleotide sequences of barley cytoplasmic glutamate transfer RNAs and structural features essential for formation of δ-aminolevulinic acid. Plant Molecular Biology 1988, 11: 293-299. PMID: 24272342, DOI: 10.1007/bf00027386.Peer-Reviewed Original ResearchChloroplast aminoacyl-tRNA synthetasesGlu-tRNA reductaseNumber of prokaryotesΔ-aminolevulinic acidMultistep enzymatic pathwayAminoacyl-tRNA synthetasesGlu-tRNATRNA discriminationTransfer RNAALA formationNucleotide sequenceALA synthesisBarley chloroplastsUniversal precursorBarley embryosChloroplastsStructural featuresEnzymatic pathwaysTRNAAlaProkaryotesSynthetasesRNAEmbryosSpecies