2002
Divergent regulation of the HEMA gene family encoding glutamyl-tRNA reductase in Arabidopsis thaliana: expression of HEMA2 is regulated by sugars, but is independent of light and plastid signalling
Ujwal ML, McCormac AC, Goulding A, Madan Kumar A, Söll D, Terry MJ. Divergent regulation of the HEMA gene family encoding glutamyl-tRNA reductase in Arabidopsis thaliana: expression of HEMA2 is regulated by sugars, but is independent of light and plastid signalling. Plant Molecular Biology 2002, 50: 81-89. PMID: 12139011, DOI: 10.1023/a:1016081114758.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde OxidoreductasesArabidopsisBase SequenceCarbohydratesDNA, PlantFructoseGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGlucoseGlucuronidaseLightMolecular Sequence DataPlants, Genetically ModifiedPlastidsPromoter Regions, GeneticRecombinant Fusion ProteinsSequence DeletionSignal TransductionSucroseConceptsGlutamyl-tRNA reductaseSynthesis pathwayLight-dependent mannerProduction of hemeKey regulatory stepL. ColPlastid signalingPlastid signalsTransgenic ArabidopsisArabidopsis thalianaHemA geneGene familyPhotosynthetic tissuesGusA expressionDeletion analysisFirst enzymeRegulatory stepALA synthesisHEMA2HEMA1Fusion constructsBp fragmentDivergent regulationArabidopsisPromoter
2001
Regulation of HEMA1 expression by phytochrome and a plastid signal during de‐etiolation in Arabidopsis thaliana
McCormac A, Fischer A, Kumar A, Söll D, Terry M. Regulation of HEMA1 expression by phytochrome and a plastid signal during de‐etiolation in Arabidopsis thaliana. The Plant Journal 2001, 25: 549-561. PMID: 11309145, DOI: 10.1046/j.1365-313x.2001.00986.x.Peer-Reviewed Original ResearchConceptsPhotosynthesis-related nuclear genesRNA gel blot analysisTetrapyrrole biosynthetic genesTransgenic Arabidopsis linesGlutamyl-tRNA reductaseGel blot analysisLow-fluence response modeRoots of seedlingsPlastid signalsArabidopsis linesNuclear genesArabidopsis thalianaPlant tetrapyrrolesBiosynthetic genesHemA genePhytochrome familyPhotosynthetic tissuesGusA expressionChlorophyll accumulationFactor signalsPromoter fragmentCis elementsALA synthesisTranscriptional levelPromoter constructs
2000
Antisense HEMA1 RNA Expression Inhibits Heme and Chlorophyll Biosynthesis in Arabidopsis1
Kumar A, Söll D. Antisense HEMA1 RNA Expression Inhibits Heme and Chlorophyll Biosynthesis in Arabidopsis1. Plant Physiology 2000, 122: 49-56. PMID: 10631248, PMCID: PMC58843, DOI: 10.1104/pp.122.1.49.Peer-Reviewed Original ResearchConceptsConstitutive cauliflower mosaic virus 35S promoterCauliflower mosaic virus 35S promoterTransgenic Arabidopsis plantsGlutamyl-tRNA reductaseBiosynthesis of tetrapyrrolesNormal growth conditionsLevels of chlorophyllFormation of ALAArabidopsis plantsChlorophyll biosynthesisHemA geneChlorophyll deficiencyGsa geneFirst enzymeGene expressionEnzymatic stepsSecond enzymeHeme synthesisPlantsReductase expressionChlorophyllGrowth conditionsBiosynthesisHemeGenes
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
1992
Arabidopsis alternative oxidase sustains Escherichia coli respiration.
Kumar A, Söll D. Arabidopsis alternative oxidase sustains Escherichia coli respiration. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 10842-10846. PMID: 1438286, PMCID: PMC50438, DOI: 10.1073/pnas.89.22.10842.Peer-Reviewed Original ResearchConceptsAlternative oxidaseArabidopsis thaliana cDNA libraryGlutamyl-tRNA reductaseCyanide-insensitive respiratory pathwayAlternative oxidase activityAmino acid sequenceArabidopsis proteinsHemA geneMolecular biological investigationsCDNA libraryFirst enzymeAcid sequenceSauromatum guttatumEscherichia coli strainsSingle polypeptideRespiratory pathwayAerobic respirationRedox enzymesE. coliColi strainsPorphyrin biosynthesisGenesEnzymeProteinBiological investigationsGlutamyl-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
Purification 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