2010
Mutations Disrupting Selenocysteine Formation Cause Progressive Cerebello-Cerebral Atrophy
Agamy O, Zeev B, Lev D, Marcus B, Fine D, Su D, Narkis G, Ofir R, Hoffmann C, Leshinsky-Silver E, Flusser H, Sivan S, Söll D, Lerman-Sagie T, Birk OS. Mutations Disrupting Selenocysteine Formation Cause Progressive Cerebello-Cerebral Atrophy. American Journal Of Human Genetics 2010, 87: 538-544. PMID: 20920667, PMCID: PMC2948803, DOI: 10.1016/j.ajhg.2010.09.007.Peer-Reviewed Original Research
2009
The Human SepSecS-tRNASec Complex Reveals the Mechanism of Selenocysteine Formation
Palioura S, Sherrer RL, Steitz TA, Söll D, Simonović M. The Human SepSecS-tRNASec Complex Reveals the Mechanism of Selenocysteine Formation. Science 2009, 325: 321-325. PMID: 19608919, PMCID: PMC2857584, DOI: 10.1126/science.1173755.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesBase SequenceBiocatalysisCatalytic DomainCrystallography, X-RayHumansHydrogen BondingModels, MolecularMolecular Sequence DataNucleic Acid ConformationPhosphatesPhosphoserineProtein ConformationProtein MultimerizationProtein Structure, SecondaryRNA, Transfer, Amino Acid-SpecificRNA, Transfer, Amino AcylSelenocysteineConceptsTransfer RNASelenocysteine formationSelenocysteinyl-tRNA synthaseCognate transfer RNAEnzyme active siteTRNA bindingActive siteConformational changesEnzyme assaysAmino acidsFree phosphoserinePhosphoserineSepSecSFinal stepSelenocysteineBiosynthesisComplexesRNAMechanismBindsCrystal structureSynthaseBindingFormationAssays
2006
Aminoacyl‐tRNAs: Deciphering and Defining the Genetic Message
Ambrogelly A, Salazar J, Sheppard K, Polycarpo C, Oshikane H, Nakamura Y, Fukai S, Nureki O, Söll D. Aminoacyl‐tRNAs: Deciphering and Defining the Genetic Message. 2006, 207-215. DOI: 10.1002/9780470750865.ch18.Peer-Reviewed Original ResearchRNA‐Dependent Cysteine Biosynthesis in Archaea
Yuan J, Sauerwald A, Zhu W, Major T, Roy H, Palioura S, Jahn D, Whitman W, Yates J, Ibba M, Söll D. RNA‐Dependent Cysteine Biosynthesis in Archaea. The FASEB Journal 2006, 20: a503-a504. DOI: 10.1096/fasebj.20.4.a503-d.Peer-Reviewed Original ResearchCysteine biosynthesisSep-tRNACys-tRNA synthaseCys-tRNACysPhosphoseryl-tRNA synthetaseCysteinyl-tRNA synthetaseCys-tRNAGenetic experimentsSec tRNAMost organismsMethanocaldococcus jannaschiiGenetic codeGenomic analysisEssential enzymeMethanogenic archaeaArchaeaSimilar enzymesO-phosphoserineBiosynthesisOrganismsSynthetaseEnzymePathwaySulfur donorSole route
2005
RNA-Dependent Cysteine Biosynthesis in Archaea
Sauerwald A, Zhu W, Major TA, Roy H, Palioura S, Jahn D, Whitman WB, Yates JR, Ibba M, Söll D. RNA-Dependent Cysteine Biosynthesis in Archaea. Science 2005, 307: 1969-1972. PMID: 15790858, DOI: 10.1126/science.1108329.Peer-Reviewed Original ResearchConceptsCysteine biosynthesisSep-tRNAComparative genomic analysisCys-tRNA synthasePhosphoseryl-tRNA synthetaseCys-tRNACysteine auxotrophyMost organismsMethanocaldococcus jannaschiiMethanococcus maripaludisGenetic codeGenomic analysisEssential enzymeO-phosphoserineBiosynthesisRNA synthetaseOrganismsSepRSSynthetasePartial purificationCysteineSole routeArchaeaSepCysSJannaschii
2004
Cys-tRNACys formation and cysteine biosynthesis in methanogenic archaea: two faces of the same problem?
Ambrogelly A, Kamtekar S, Sauerwald A, Ruan B, Tumbula-Hansen D, Kennedy D, Ahel I, Söll D. Cys-tRNACys formation and cysteine biosynthesis in methanogenic archaea: two faces of the same problem? Cellular And Molecular Life Sciences 2004, 61: 2437-2445. PMID: 15526152, DOI: 10.1007/s00018-004-4194-9.Peer-Reviewed Original ResearchConceptsMethanogenic archaeaCysteine biosynthesisCellular translation machineryAminoacyl-tRNA synthesisCanonical cysteinyl-tRNA synthetaseAminoacyl-tRNA synthetasesCysteinyl-tRNA synthetaseRecognizable genesTranslation machineryGenome sequenceArchaeaBiosynthesisEssential componentSynthetasesTRNARibosomesGenesMachineryOrganismsSynthetasePossible linkSequenceFormation
2000
Domain-specific recruitment of amide amino acids for protein synthesis
Tumbula D, Becker H, Chang W, Söll D. Domain-specific recruitment of amide amino acids for protein synthesis. Nature 2000, 407: 106-110. PMID: 10993083, DOI: 10.1038/35024120.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseAsparaginyl-tRNA synthetaseProtein synthesisAmino acidsAminoacyl-transfer RNAAmino acid metabolismGlu-tRNAGlnAsn-tRNAProtein biosynthesisGln-tRNAArchaeaTRNASynthetaseAmidotransferaseBacteriaAmidotransferasesDirect evidenceDifferent mechanismsBiosynthesisCentral importanceCrucial stepRNAOrganismsDomainCytoplasmCysteine Biosynthesis Pathway in the ArchaeonMethanosarcina barkeri Encoded by Acquired Bacterial Genes?
Kitabatake M, So M, Tumbula D, Söll D. Cysteine Biosynthesis Pathway in the ArchaeonMethanosarcina barkeri Encoded by Acquired Bacterial Genes? Journal Of Bacteriology 2000, 182: 143-145. PMID: 10613873, PMCID: PMC94250, DOI: 10.1128/jb.182.1.143-145.2000.Peer-Reviewed Original ResearchConceptsCysteine biosynthesis pathwayCysK geneCysteine biosynthesisBiosynthesis pathwayRecent genome dataOpen reading framePyrococcus sppCysE geneBacterial genesMethanococcus jannaschiiGenome dataArchaeoglobus fulgidusReading frameSulfolobus solfataricusThermoplasma acidophilumCysM geneMethanobacterium thermoautotrophicumGenesBiosynthesisPathwayGreat similaritySame functionCysKOrthologsArchaeaAntisense 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 metaboliteAlaBiosynthesisInhibitionTetrapyrrolesGlutamateArchaeal Aminoacyl-tRNA Synthesis: Diversity Replaces Dogma
Tumbula D, Vothknecht U, Kim H, Ibba M, Min B, Li T, Pelaschier J, Stathopoulos C, Becker H, Söll D. Archaeal Aminoacyl-tRNA Synthesis: Diversity Replaces Dogma. Genetics 1999, 152: 1269-1276. PMID: 10430557, PMCID: PMC1460689, DOI: 10.1093/genetics/152.4.1269.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthesisGene transfer eventsPhenylalanyl-tRNA synthetasesLysyl-tRNA synthetaseTransamidation pathwayExtant organismsMethanococcus jannaschiiAsparaginyl-tRNAProtein biosynthesisGenetic codeGene expressionGenome sequencingAminoacyl-tRNAArchaeaMethanobacterium thermoautotrophicumMolecular biologyUnexpected levelNovel pathwayTransfer eventsFaithful translationPathwayJannaschiiSynthetasesBiosynthesisOrganisms
1998
Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis
Curnow A, Tumbula D, Pelaschier J, Min B, Söll D. Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 12838-12843. PMID: 9789001, PMCID: PMC23620, DOI: 10.1073/pnas.95.22.12838.Peer-Reviewed Original ResearchConceptsDeinococcus radioduransD. radiodurans genomeRadiation-resistant bacterium Deinococcus radioduransBiosynthesis of asparagineGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseBacterium Deinococcus radioduransPresence of AsnRSAsparaginyl-tRNA synthetaseAspartyl-tRNA synthetaseAsn-tRNAAsparagine biosynthesisAsparaginyl-tRNAGenomic sequencesGln-tRNAAsparagine synthetaseBiochemical experimentsTransamidation activityGlutaminyl-tRNAProtein synthesisSingle enzymeSynthetaseRadioduransBiosynthesisGenes
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 precursorBiosynthesesGenesRNAProteinReductaseChlorophyllEnzymeRegulationAla
1994
Transfer RNA in Its Fourth Decade
RajBhandary U, Söll D. Transfer RNA in Its Fourth Decade. 1994, 1-4. DOI: 10.1128/9781555818333.ch1.Peer-Reviewed Original ResearchA 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, 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 ResearchCompetition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation
Sherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 2847-2852. PMID: 1377381, PMCID: PMC336931, DOI: 10.1093/nar/20.11.2847.Peer-Reviewed Original ResearchConceptsAccuracy of aminoacylationAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetaseE. coli tyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetaseGlutaminyl-tRNA synthetaseLevel of aminoacylationProtein biosynthesisTRNASynthetasesAminoacylationCompetition assaysDiscriminator baseDifferent synthetasesConcurrent overexpressionCorrect aminoacylationSynthetaseFirst baseRelative affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetitionCompetition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation
Sherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 1547-1552. PMID: 16617497, PMCID: PMC312236, DOI: 10.1093/nar/20.7.1547.Peer-Reviewed Original ResearchAccuracy of aminoacylationAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetaseE. coli tyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetaseGlutaminyl-tRNA synthetaseLevel of aminoacylationProtein biosynthesisTRNASynthetasesAminoacylationCompetition assaysDiscriminator baseDifferent synthetasesConcurrent overexpressionCorrect aminoacylationSynthetaseFirst baseRelative affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetition
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 system