Search results for "Saccharomyces cerevisiae Proteins"

showing 10 items of 231 documents

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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A sequence element downstream of the yeast HTB1 gene contributes to mRNA 3' processing and cell cycle regulation.

2002

Histone mRNAs accumulate in the S phase and are rapidly degraded as cells progress into the G(2) phase of the cell cycle. In Saccharomyces cerevisiae, fusion of the 3' untranslated region and downstream sequences of the yeast histone gene HTB1 to a neomycin phosphotransferase open reading frame is sufficient to confer cell cycle regulation on the resulting chimera gene (neo-HTB1). We have identified a sequence element, designated the distal downstream element (DDE), that influences both the 3'-end cleavage site selection and the cell cycle regulation of the neo-HTB1 mRNA. Mutations in the DDE, which is located approximately 110 nucleotides downstream of the HTB1 gene, lead to a delay in the…

Untranslated regionSaccharomyces cerevisiae ProteinsGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeGene ExpressionSaccharomyces cerevisiaeRegulatory Sequences Nucleic AcidPrimary transcriptHistonesOpen Reading FramesGene Expression Regulation FungalMolecular BiologyGeneS phaseBase SequencebiologyCell CycleSingle-Strand Specific DNA and RNA EndonucleasesCell BiologyCell cyclebiology.organism_classificationMolecular biologyDNA-Binding ProteinsHistoneMutagenesis Site-Directedbiology.proteinNucleic Acid ConformationRNA 3' End ProcessingG1 phase
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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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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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Membrane topology and post-translational modification of the Saccharomyces cerevisiae essential protein Rot1.

2007

ROT1 is an essential gene that has been related to cell wall biosynthesis, the actin cytoskeleton and protein folding. In order to help to understand its molecular function, we carried out a characterization of the Rot1 protein. It is primarily located at the endoplasmic reticulum-nuclear membrane facing the lumen. Rot1 migrates more slowly than expected, which might suggest post-translational modification. Our results indicate that Rot1 is a protein that is neither GPI-anchored nor O-glycosylated. In contrast, it is N-glycosylated. By a directed mutagenesis of several Asn residues, we identified that the protein is simultaneously glycosylated at N103, N107 and N139. Although the mutation o…

Vesicle-associated membrane protein 8Saccharomyces cerevisiae ProteinsMolecular Sequence DataBioengineeringmacromolecular substancesSaccharomyces cerevisiaeBiologyEndoplasmic ReticulumApplied Microbiology and BiotechnologyBiochemistryProtein structureSEC62Gene Expression Regulation FungalGeneticsAmino Acid SequenceCell MembraneMembrane ProteinsActin cytoskeletonCell biologyTransport proteinProtein Structure TertiaryTransmembrane domainProtein TransportBiochemistryMembrane topologyProtein foldingProtein Processing Post-TranslationalBiotechnologyMolecular ChaperonesYeast (Chichester, England)
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Population Structure and Comparative Genome Hybridization of European Flor Yeast Reveal a Unique Group of Saccharomyces cerevisiae Strains with Few G…

2014

Wine biological aging is a wine making process used to produce specific beverages in several countries in Europe, including Spain, Italy, France, and Hungary. This process involves the formation of a velum at the surface of the wine. Here, we present the first large scale comparison of all European flor strains involved in this process. We inferred the population structure of these European flor strains from their microsatellite genotype diversity and analyzed their ploidy. We show that almost all of these flor strains belong to the same cluster and are diploid, except for a few Spanish strains. Comparison of the array hybridization profile of six flor strains originating from these four co…

[SDV.SA]Life Sciences [q-bio]/Agricultural scienceslcsh:MedicineArray CGHespagneyeastbrewer sGenomeComputational biologyPloidymicrobial floraGene DuplicationGenotypevinCluster Analysissaccharomyces cerevisiaelcsh:SciencePhylogenySequence DeletionGenetics0303 health sciencesComparative Genomic HybridizationMultidisciplinaryVegetal BiologyMembrane GlycoproteinsEcologyAlcoholic BeveragesMicrobial GeneticshongrieGenomicsBiodiversityAgricultural sciencesoenologieMicrosatellitePloidyGenome FungalgénotypefranceResearch ArticleSaccharomyces cerevisiae ProteinsMolecular Sequence DataFlorflore microbiennevieillissement vinBiologyMicrobiologyMicrobial EcologyBeverages03 medical and health sciencesSaccharomycesGenetic variationGenetics[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyAmino Acid Sequencewinemicrobiologie030304 developmental biologyNutritionComparative genomicsWineEvolutionary BiologyBase SequenceBiology and life sciences030306 microbiologylcsh:ROrganismsFungiGenetic VariationGenome analysisDietitalieGenetic LociBiofilmsGenetic Polymorphismlcsh:QSequence AlignmentSciences agricolesBiologie végétalePopulation GeneticsMicrosatellite Repeats
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Comparative analysis of the coordinated motion of Hsp70s from different organelles observed by single-molecule three-color FRET.

2021

Cellular function depends on the correct folding of proteins inside the cell. Heat-shock proteins 70 (Hsp70s), being among the first molecular chaperones binding to nascently translated proteins, aid in protein folding and transport. They undergo large, coordinated intra- and interdomain structural rearrangements mediated by allosteric interactions. Here, we applied a three-color single-molecule Forster resonance energy transfer (FRET) combined with three-color photon distribution analysis to compare the conformational cycle of the Hsp70 chaperones DnaK, Ssc1, and BiP. By capturing three distances simultaneously, we can identify coordinated structural changes during the functional cycle. Be…

chemistry.chemical_classificationOrganellesMultidisciplinarySaccharomyces cerevisiae ProteinsAllosteric regulationPeptideSaccharomyces cerevisiaeBiological SciencesMitochondrial Membrane Transport ProteinsRecombinant ProteinsSingle Molecule ImagingFolding (chemistry)Förster resonance energy transferchemistryHeat shock proteinBiophysicsEscherichia coliFluorescence Resonance Energy TransferMoleculeProtein foldingNucleotideHSP70 Heat-Shock ProteinsMolecular ChaperonesProceedings of the National Academy of Sciences of the United States of America
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Identification of a Functional Homolog of the Yeast Copper Homeostasis Gene ATX1 from Arabidopsis1

1998

Abstract A cDNA clone encoding a homolog of the yeast (Saccharomyces cerevisiae) gene Anti-oxidant 1(ATX1) has been identified from Arabidopsis. This gene, referred to as CopperCHaperone(CCH), encodes a protein that is 36% identical to the amino acid sequence of ATX1 and has a 48-amino acid extension at the C-terminal end, which is absent from ATX1 homologs identified in animals. ATX1-deficient yeast (atx1) displayed a loss of high-affinity iron uptake. Expression of CCH in the atx1 strain restored high-affinity iron uptake, demonstrating thatCCH is a functional homolog of ATX1. When overexpressed in yeast lacking the superoxide dismutase geneSOD1, both ATX1 and CCHprotected the cell from t…

endocrine systemDNA ComplementarySaccharomyces cerevisiae ProteinsPhysiologyMolecular Sequence DataSaccharomyces cerevisiaeSOD1ArabidopsisGene ExpressionSaccharomyces cerevisiaePlant ScienceFungal ProteinsGene productSuperoxide dismutaseOzoneCopper Transport ProteinsComplementary DNAArabidopsisGene expressionGeneticsHomeostasisAmino Acid SequenceCation Transport ProteinsBase SequenceSequence Homology Amino AcidbiologyArabidopsis ProteinsGenetic Complementation Testbiology.organism_classificationYeastOxidative StressBiochemistrybiology.proteinCarrier ProteinsCopperResearch ArticlePlant Physiology
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Xrn1 influence on gene transcription results from the combination of general effects on elongating RNA pol II and gene-specific chromatin configurati…

2020

mRNA homoeostasis is favoured by crosstalk between transcription and degradation machineries. Both the Ccr4-Not and the Xrn1-decaysome complexes have been described to influence transcription. While Ccr4-Not has been shown to directly stimulate transcription elongation, the information available on how Xrn1 influences transcription is scarce and contradictory. In this study we have addressed this issue by mapping RNA polymerase II (RNA pol II) at high resolution, using CRAC and BioGRO-seq techniques in Saccharomyces cerevisiae. We found significant effects of Xrn1 perturbation on RNA pol II profiles across the genome. RNA pol II profiles at 5ʹ exhibited significant alterations that were com…

mRNA bufferingSaccharomyces cerevisiae ProteinsTranscription Elongation GeneticTranscription elongationPolyadenylationSaccharomyces cerevisiaeMRNA DecayRNA polymerase IISaccharomyces cerevisiaeTranscription elongation03 medical and health sciences0302 clinical medicinemRNA decayTranscription (biology)RNA decay/gene transcription crosstalkGene Expression Regulation FungalNucleosomemRNA decay/gene transcription crosstalkMolecular BiologyXrn1Gene030304 developmental biology0303 health sciencesMessenger RNAbiologyChemistryCell Biologybiology.organism_classificationRNA bufferingmChromatinChromatinCell biologyNucleosomesCrosstalk (biology)3ʹ pre-mRNA processing030220 oncology & carcinogenesisXrn13ʹExoribonucleasesbiology.proteinpre-mRNA processingmRNA Polymerase IITranscriptional Elongation FactorsResearch PaperRNA biology
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Eukaryotic rRNA Modification by Yeast 5-Methylcytosine-Methyltransferases and Human Proliferation-Associated Antigen p120.

2015

International audience; Modified nucleotide 5-methylcytosine (m(5)C) is frequently present in various eukaryotic RNAs, including tRNAs, rRNAs and in other non-coding RNAs, as well as in mRNAs. RNA: m(5)C-methyltranferases (MTases) Nop2 from S. cerevisiae and human proliferation-associated nucleolar antigen p120 are both members of a protein family called Nop2/NSUN/NOL1. Protein p120 is well-known as a tumor marker which is over-expressed in various cancer tissues. Using a combination of RNA bisulfite sequencing and HPLC-MS/MS analysis, we demonstrated here that p120 displays an RNA:m(5)C-MTase activity, which restores m(5)C formation at position 2870 in domain V of 25S rRNA in a nop2 Delta …

tRNA MethyltransferasesSaccharomyces cerevisiae Proteinslcsh:RNuclear Proteinslcsh:MedicineMethyltransferasesSaccharomyces cerevisiaeProtein Structure TertiaryRNA Ribosomal5-MethylcytosineHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biologylcsh:Qlcsh:Science[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyProtein BindingResearch ArticlePLoS ONE
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