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
1996
Glutamyl-transfer RNA: at the crossroad between chlorophyll and protein biosynthesis
Kumar A, Schaub U, Söll D, Ujwal M. Glutamyl-transfer RNA: at the crossroad between chlorophyll and protein biosynthesis. Trends In Plant Science 1996, 1: 371-376. DOI: 10.1016/s1360-1385(96)80311-6.Peer-Reviewed Original ResearchTransfer RNAConversion of GSAGlu-tRNA reductaseEssential biosynthetic processesVariety of plantsChlorophyll biosynthesisGlu-tRNAHigher plantsProtein biosynthesisBiosynthetic processesBiosynthesisPlantsPivotal stepFirst pivotal stepChloroplastsKey precursorBiosynthesesGenesRNAProteinReductaseChlorophyllEnzymeRegulationAlaA 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 enzymeLight Regulation of Chlorophyll Biosynthesis at the Level of 5-Aminolevulinate Formation in Arabidopsis
Ilag L, Kumar A, Soll D. Light Regulation of Chlorophyll Biosynthesis at the Level of 5-Aminolevulinate Formation in Arabidopsis. The Plant Cell 1994, 6: 265. DOI: 10.2307/3869644.Peer-Reviewed Original Research
1992
Chloroplast tRNAAsp: nucleotide sequence and variation of in vivo levels during plastid maturation
Schön A, Gough S, Söll D. Chloroplast tRNAAsp: nucleotide sequence and variation of in vivo levels during plastid maturation. Plant Molecular Biology 1992, 20: 601-607. PMID: 1450377, DOI: 10.1007/bf00046445.Peer-Reviewed Original Research
1991
Transfer 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 ResearchConceptsTransfer RNARegulation of hemeBranched biosynthetic pathwayPorphyrin biosynthesisBiosynthesis of ALAPhotosynthetic metabolismChlorophyll biosynthesisRNA involvementArchaebacterial kingdomMammalian cellsBiosynthetic pathwayChlorophyll synthesisBacterial systemsBiosynthesisRecent rapid progressPlantsCentral roleAlaHemeTetrapyrrole ringEnzymePathwayFive-carbonProkaryotesExperimental systemPurification 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
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 acidTRNAChlorophyllPurification 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
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