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 ResearchMeSH KeywordsAldehyde OxidoreductasesArabidopsisBlotting, NorthernBlotting, WesternChlorophyllChromosome MappingHemePlants, Genetically ModifiedRNA, AntisenseConceptsConstitutive 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 ResearchMeSH KeywordsAldehyde OxidoreductasesAminolevulinic AcidArabidopsisGene Expression Regulation, PlantGlutamic AcidOxidation-ReductionPhotochemistryConceptsArabidopsis 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
A point mutation in Euglena gracilis chloroplast tRNA(Glu) uncouples protein and chlorophyll biosynthesis.
Stange-Thomann N, Thomann H, Lloyd A, Lyman H, Söll D. A point mutation in Euglena gracilis chloroplast tRNA(Glu) uncouples protein and chlorophyll biosynthesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 7947-7951. PMID: 8058739, PMCID: PMC44521, DOI: 10.1073/pnas.91.17.7947.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde OxidoreductasesAnimalsBase SequenceBlotting, NorthernChlorophyllChloroplastsCloning, MolecularDNADNA PrimersEuglena gracilisIntramolecular TransferasesIsomerasesMolecular Sequence DataNucleic Acid ConformationPoint MutationPolymerase Chain ReactionProtein BiosynthesisRNA, Transfer, GluConceptsEuglena gracilis chloroplastsChlorophyll biosynthesisGlu-tRNA reductaseChlorophyll-deficient mutantsPoint mutationsChloroplast protein synthesisSequence-specific mannerDual-function moleculeC5 pathwayNADPH-dependent reductionSpecific cofactorsGluTRFirst enzymeGene productsUniversal precursorImportant identity elementAminomutase activitySequence analysisE. gracilisSecond enzymeTetrapyrrole pigmentsT-loopProtein synthesisBiosynthesisChloroplastsLight 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
The periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli
Verkamp E, Backman V, Björnsson J, Söll D, Eggertsson G. The periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli. Journal Of Bacteriology 1993, 175: 1452-1456. PMID: 8444807, PMCID: PMC193232, DOI: 10.1128/jb.175.5.1452-1456.1993.Peer-Reviewed Original ResearchConceptsDpp operonE. coli chromosomeEscherichia coliWild-type growthClasses of mutantsAbsence of ALAGenetic screenDpp mutationsColi chromosomeDpp transportALA biosynthesisFirst geneDipeptide transport systemAnaerobic growthChromosomal insertionOperonRecombinant plasmidTransport systemExogenous ALAALA uptakeE. coliNormal growthMutantsMutationsColi
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
1990
Transfer RNA and the formation of the heme and chlorophyll precursor, 5-aminolevulinic acid.
O'Neill G, Söll D. Transfer RNA and the formation of the heme and chlorophyll precursor, 5-aminolevulinic acid. BioFactors 1990, 2: 227-35. PMID: 2282139.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde OxidoreductasesAminolevulinic AcidBase SequenceChlorophyllGlutamate-tRNA LigaseHemeMolecular Sequence DataNucleic Acid ConformationRNA, Transfer, GluConceptsGlu-tRNA reductaseSequence-specific recognitionDual-function moleculeNADPH-dependent enzymeThree-step pathwayTransfer RNASpecific cofactorsChlorophyll precursorsLow molecular weight metabolitesNovel roleAmino acidsReduction of glutamatePeptide bond synthesisTRNAWeight metabolitesHemeMetabolic conversionBond synthesisBiosynthesisRNAOrganismsAcidCofactorProteinGlutamate