0000000000417325

AUTHOR

Dennis J. Thiele

showing 9 related works from this author

Higher plants possess two different types of ATX1-like copper chaperones.

2007

Abstract Copper (Cu) chaperones constitute a family of small Cu+-binding proteins required for Cu homeostasis in eukaryotes. The ATX1 family of Cu chaperones specifically delivers Cu to heavy metal P-type ATPases. The plant Arabidopsis thaliana expresses the ATX1-like Cu chaperone CCH, which exhibits a plant-specific carboxy-terminal domain (CTD) with unique structural properties. We show that CCH homologues from other higher plants contain CTDs with structural properties similar to Arabidopsis CCH. Furthermore, we identify a new ATX1-like Cu chaperone in Arabidopsis, AtATX1, which functionally complements yeast atx1Δ and sod1Δ associated phenotypes, and localizes to the cytosol of Arabidop…

endocrine systemATPaseTwo-hybrid screeningBiophysicsArabidopsischemistry.chemical_elementBiochemistryArabidopsisMolecular BiologyAdenosine TriphosphatasesbiologyArabidopsis ProteinsCell BiologyHistone-Lysine N-Methyltransferasebiology.organism_classificationPhenotypeCopperYeastProtein Structure TertiaryCytosolBiochemistrychemistryChaperone (protein)biology.proteinCopperGenome PlantMolecular ChaperonesTranscription FactorsBiochemical and biophysical research communications
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Dissection of the relative contribution of the Schizosaccharomyces pombe Ctr4 and Ctr5 proteins to the copper transport and cell surface delivery fun…

2011

The Ctr1 family of proteins mediates high-affinity copper (Cu) acquisition in eukaryotic organisms. In the fission yeastSchizosaccharomyces pombe, Cu uptake is carried out by a heteromeric complex formed by the Ctr4 and Ctr5 proteins. Unlike human andSaccharomyces cerevisiaeCtr1 proteins, Ctr4 and Ctr5 are unable to function independently in Cu acquisition. Instead, both proteins physically interact with each other to form a Ctr4–Ctr5 heteromeric complex, and are interdependent for secretion to the plasma membrane and Cu transport activity. In this study, we usedS. cerevisiaemutants that are defective in high-affinity Cu uptake to dissect the relative contribution of Ctr4 and Ctr5 to the Cu…

Amino Acid MotifsMutantSaccharomyces cerevisiaeSaccharomyces cerevisiaeBiologyMicrobiologySchizosaccharomycesHumansSecretionAmino Acid SequenceSLC31 ProteinsCation Transport ProteinsCell MembraneGenetic Complementation Testbiology.organism_classificationFusion proteinYeastProtein Structure TertiaryCell biologyComplementationTransmembrane domainBiochemistryCell and Molecular Biology of MicrobesSchizosaccharomyces pombeSchizosaccharomyces pombe ProteinsSequence AlignmentCopper
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Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation.

2004

AbstractIron (Fe) is an essential micronutrient for virtually all organisms and serves as a cofactor for a wide variety of vital cellular processes. Although Fe deficiency is the primary nutritional disorder in the world, cellular responses to Fe deprivation are poorly understood. We have discovered a posttranscriptional regulatory process controlled by Fe deficiency, which coordinately drives widespread metabolic reprogramming. We demonstrate that, in response to Fe deficiency, the Saccharomyces cerevisiae Cth2 protein specifically downregulates mRNAs encoding proteins that participate in many Fe-dependent processes. mRNA turnover requires the binding of Cth2, an RNA binding protein conser…

Untranslated regionSaccharomyces cerevisiae ProteinsTranscription GeneticIronSaccharomyces cerevisiaeMolecular Sequence DataDown-RegulationRNA-binding proteinSaccharomyces cerevisiaeBiologyGeneral Biochemistry Genetics and Molecular BiologyCofactorTristetraprolinGene Expression Regulation FungalMRNA degradationmedicineRNA MessengerRNA Processing Post-TranscriptionalMessenger RNABase SequenceBiochemistry Genetics and Molecular Biology(all)Mechanism (biology)Iron deficiencybiology.organism_classificationmedicine.diseaseDNA-Binding ProteinsBiochemistryMutationbiology.proteinPlasmidsCell
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The Arabidopsis heavy metal P-type ATPase HMA5 interacts with metallochaperones and functions in copper detoxification of roots

2005

*† ‡ § Summary Since copper (Cu) is essential in key physiological oxidation reactions, organisms have developed strategies for handling Cu while avoiding its potentially toxic effects. Among the tools that have evolved to cope with Cu is a network of Cu homeostasis factors such as Cu-transporting P-type ATPases that play a key role in transmembrane Cu transport. In this work we present the functional characterization of an Arabidopsis Cutransporting P-type ATPase, denoted heavy metal ATPase 5 (HMA5), and its interaction with Arabidopsis metallochaperones. HMA5 is primarily expressed in roots, and is strongly and specifically induced by Cu in whole plants. We have identified and characteriz…

ATPaseMolecular Sequence DataMutantArabidopsisPlant ScienceGenes PlantPlant RootsMetallochaperonesArabidopsisGeneticsAmino Acid SequenceRNA MessengerDNA PrimersAdenosine TriphosphatasesBase SequenceSequence Homology Amino AcidbiologyArabidopsis ProteinsCell BiologyCompartmentalization (fire protection)biology.organism_classificationTransmembrane proteinCell biologyBiochemistryChaperone (protein)biology.proteinP-type ATPaseCopperMolecular ChaperonesThe Plant Journal
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Negative feedback regulation of the yeast CTH1 and CTH2 mRNA binding proteins is required for adaptation to iron deficiency and iron supplementation.

2013

Iron (Fe) is an essential element for all eukaryotic organisms because it functions as a cofactor in a wide range of biochemical processes. Cells have developed sophisticated mechanisms to tightly control Fe utilization in response to alterations in cellular demands and bioavailability. In response to Fe deficiency, the yeast Saccharomyces cerevisiae activates transcription of the CTH1 and CTH2 genes, which encode proteins that bind to AU-rich elements (AREs) within the 3′ untranslated regions (3′UTRs) of many mRNAs, leading to metabolic reprogramming of Fe-dependent pathways and decreased Fe storage. The precise mechanisms underlying Cth1 and Cth2 function and regulation are incompletely u…

Untranslated regionSaccharomyces cerevisiae ProteinsIronRNA StabilitySaccharomyces cerevisiaeMolecular Sequence DataSaccharomyces cerevisiaeBiologyCofactorTristetraprolinIn vivoTranscription (biology)Gene Expression Regulation FungalAutoregulationRNA MessengerMolecular BiologyGene3' Untranslated RegionsAU Rich ElementsBase SequenceCell BiologyArticlesbiology.organism_classificationMolecular biologyAdaptation PhysiologicalYeastCell biologyDNA-Binding Proteinsbiology.proteinTranscription FactorsMolecular and cellular biology
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Cooperation of Two mRNA-Binding Proteins Drives Metabolic Adaptation to Iron Deficiency

2008

Summary Iron (Fe) is an essential cofactor for a wide range of cellular processes. We have previously demonstrated in yeast that Cth2 is expressed during Fe deficiency and promotes degradation of a battery of mRNAs leading to reprogramming of Fe-dependent metabolism and Fe storage. We report here that the Cth2-homologous protein Cth1 is transiently expressed during Fe deprivation and participates in the response to Fe deficiency through the degradation of mRNAs primarily involved in mitochondrially localized activities including respiration and amino acid biosynthesis. In parallel, wild-type cells, but not cth1 Δ cth2 Δ cells, accumulate mRNAs encoding proteins that function in glucose impo…

Saccharomyces cerevisiae ProteinsPhysiologySaccharomyces cerevisiaeHUMDISEASERNA-binding proteinSaccharomyces cerevisiaeProtein Serine-Threonine KinasesDNA-binding proteinArticlechemistry.chemical_compoundTristetraprolinGlucose importRNA MessengerPhosphorylationProtein kinase AMolecular BiologybiologyGlycogenRNA-Binding ProteinsIron DeficienciesCell BiologyMetabolismbiology.organism_classificationAdaptation PhysiologicalDNA-Binding ProteinsMetabolismBiochemistrychemistryPhosphorylationTranscription FactorsCell Metabolism
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The Cth2 ARE-binding protein recruits the Dhh1 helicase to promote the decay of succinate dehydrogenase SDH4 mRNA in response to iron deficiency

2008

Iron is an essential nutrient that participates as a redox co-factor in a broad range of cellular processes. In response to iron deficiency, the budding yeast Saccharomyces cerevisiae induces the expression of the Cth1 and Cth2 mRNA-binding proteins to promote a genome-wide remodeling of cellular metabolism that contributes to the optimal utilization of iron. Cth1 and Cth2 proteins bind to specific AU-rich elements within the 3'-untranslated region of many mRNAs encoding proteins involved in iron-dependent pathways, thereby promoting their degradation. Here, we show that the DEAD box Dhh1 helicase plays a crucial role in the mechanism of Cth2-mediated mRNA turnover. Yeast two-hybrid experim…

Untranslated regionCytoplasmSaccharomyces cerevisiae ProteinsDEAD boxIronSaccharomyces cerevisiaeSaccharomyces cerevisiaeRNA-Mediated Regulation and Noncoding RnasModels BiologicalBiochemistryDEAD-box RNA HelicasesTristetraprolinGene Expression Regulation FungalTwo-Hybrid System TechniquesP-bodiesRNA MessengerMolecular BiologyMessenger RNAbiologySuccinate dehydrogenaseBinding proteinGalactoseHelicaseCell Biologybiology.organism_classificationProtein Structure TertiarySuccinate DehydrogenaseGlucoseBiochemistryMutationbiology.proteinPlasmids
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The Arabidopsis Copper Transporter COPT1 Functions in Root Elongation and Pollen Development

2004

Copper plays a dual role in aerobic organisms, as both an essential and a potentially toxic element. To ensure copper availability while avoiding its toxic effects, organisms have developed complex homeostatic networks to control copper uptake, distribution, and utilization. In eukaryotes, including yeasts and mammals, high affinity copper uptake is mediated by the Ctr family of copper transporters. This work is the first report on the physiological function of copper transport in Arabidopsis thaliana. We have studied the expression pattern of COPT1 in transgenic plants expressing a reporter gene under the control of the COPT1 promoter. The reporter gene is highly expressed in embryos, tric…

TransgeneArabidopsisDown-Regulationchemistry.chemical_elementPlant RootsBiochemistrychemistry.chemical_compoundGenes ReporterArabidopsisArabidopsis thalianaRNA MessengerTransgenesMolecular BiologyCopper Transporter 1Reporter geneDose-Response Relationship DrugbiologyArabidopsis ProteinsReverse Transcriptase Polymerase Chain ReactionMembrane Transport ProteinsBiological TransportTransporterCell BiologyOligonucleotides AntisensePlants Genetically Modifiedbiology.organism_classificationCopperTrichomeUp-RegulationBiochemistrychemistryMicroscopy Electron ScanningPollenGrowth inhibitionCopperPhenanthrolinesPlasmidsJournal of Biological Chemistry
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Phosphorylation and proteasome recognition of the mRNA- binding protein Cth2 facilitates yeast adaptation to iron deficiency

2018

Iron is an indispensable micronutrient for all eukaryotic organisms due to its participation as a redox cofactor in many metabolic pathways. Iron imbalance leads to the most frequent human nutritional deficiency in the world. Adaptation to iron limitation requires a global reorganization of the cellular metabolism directed to prioritize iron utilization for essential processes. In response to iron scarcity, the conserved Saccharomyces cerevisiae mRNA-binding protein Cth2, which belongs to the tristetraprolin family of tandem zinc finger proteins, coordinates a global remodeling of the cellular metabolism by promoting the degradation of multiple mRNAs encoding highly iron-consuming proteins.…

0301 basic medicineProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsIronPosttranslational regulationSaccharomyces cerevisiaeMrna bindingMicrobiology03 medical and health sciencesProtein stabilityTristetraprolinGene Expression Regulation FungalVirologyPolitical scienceProtein stabilitySerineRNA MessengerPhosphorylationIron deficiencyAdaptation PhysiologicalQR1-502Yeast030104 developmental biologyMutagenesisChristian ministryProtein Processing Post-TranslationalHumanities
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