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
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
Glutamate transfer RNA: a cofactor for heme and chlorophyll biosynthesis.
Madan Kumar A, Söll D. Glutamate transfer RNA: a cofactor for heme and chlorophyll biosynthesis. Indian Journal Of Biochemistry And Biophysics 1996, 33: 30-4. PMID: 8744830.Peer-Reviewed Original Research
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
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
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 GTPTransfer RNA Involvement in Chlorophyll Biosynthesis
O’Neill G, Jahn D, Söll D. Transfer RNA Involvement in Chlorophyll Biosynthesis. Subcellular Biochemistry 1991, 17: 235-264. PMID: 1796486, DOI: 10.1007/978-1-4613-9365-8_11.Peer-Reviewed Original ResearchMeSH KeywordsAminolevulinic AcidBacteriaBase SequenceChlorophyllGene Expression RegulationMolecular Sequence DataPlantsRNA, TransferConceptsTransfer RNARegulation of hemeBranched biosynthetic pathwayPorphyrin biosynthesisBiosynthesis of ALAPhotosynthetic metabolismChlorophyll biosynthesisRNA involvementArchaebacterial kingdomMammalian cellsBiosynthetic pathwayChlorophyll synthesisBacterial systemsBiosynthesisRecent rapid progressPlantsCentral roleAlaHemeTetrapyrrole ringEnzymePathwayFive-carbonProkaryotesExperimental systemdelta-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
1990
Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis
O'Neill G, Söll D. Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis. Journal Of Bacteriology 1990, 172: 6363-6371. PMID: 2121711, PMCID: PMC526821, DOI: 10.1128/jb.172.11.6363-6371.1990.Peer-Reviewed Original ResearchConceptsSynechocystis 6803Synechocystis spFirst anticodon baseStrain PCC 6803Cyanobacterium Synechocystis spTotal tRNA populationAmount of chlorophyllNorthern blot analysisChlorophyll biosynthesisALA biosynthesisPrecursor tRNAsPCC 6803TRNA speciesProtein biosynthesisTRNA populationCellular RNAAminoacylation assaysChlorophyll levelsBiosynthesisAddition of inhibitorsBlot analysisTranslation systemDelta-aminolevulinic acidTRNAChlorophyllTransfer 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 ResearchConceptsGlu-tRNA reductaseSequence-specific recognitionDual-function moleculeNADPH-dependent enzymeThree-step pathwayTransfer RNASpecific cofactorsChlorophyll precursorsLow molecular weight metabolitesNovel roleAmino acidsReduction of glutamatePeptide bond synthesisTRNAWeight metabolitesHemeMetabolic conversionBond synthesisBiosynthesisRNAOrganismsAcidCofactorProteinGlutamatePurification 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
delta-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
1988
Formation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species
O'Neill G, Peterson D, Schön A, Chen M, Söll D. Formation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species. Journal Of Bacteriology 1988, 170: 3810-3816. PMID: 2900830, PMCID: PMC211375, DOI: 10.1128/jb.170.9.3810-3816.1988.Peer-Reviewed Original ResearchConceptsPrecursor delta-aminolevulinic acidHigher plantsUnicellular cyanobacterium Synechocystis spGlutamate-1-semialdehyde aminotransferaseCell extractsCyanobacterium Synechocystis spDelta-aminolevulinic acidSouthern blot analysisIdentical primary sequencesSynechocystis spNucleotide modificationsConversion of glutamateGene copiesALA synthesisPrimary sequenceSequence specificityTerminal enzymePolyacrylamide gel electrophoresisChloroplastsEuglena gracilisEscherichia coliSpeciesBlot analysisTRNAGel electrophoresis
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