0000000000681518

AUTHOR

Mingxia Huang

showing 2 related works from this author

Regulation of ribonucleotide reductase in response to iron deficiency

2011

Ribonucleotide reductase (RNR) is an essential enzyme required for DNA synthesis and repair. Although iron is necessary for class Ia RNR activity, little is known about the mechanisms that control RNR in response to iron deficiency. In this work, we demonstrate that yeast cells control RNR function during iron deficiency by redistributing the Rnr2–Rnr4 small subunit from the nucleus to the cytoplasm. Our data support a Mec1/Rad53-independent mechanism in which the iron-regulated Cth1/Cth2 mRNA-binding proteins specifically interact with the WTM1 mRNA in response to iron scarcity, and promote its degradation. The resulting decrease in the nuclear-anchoring Wtm1 protein levels leads to the re…

CytoplasmSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleoside Diphosphate ReductaseRNA StabilityProtein subunitSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeProtein Serine-Threonine KinasesBiologyResponse ElementsArticleTristetraprolinGene Expression Regulation FungalRibonucleotide ReductasesHumansRNA MessengerMolecular BiologyTranscription factorCell NucleusDNA synthesisIntracellular Signaling Peptides and ProteinsFungal geneticsRNA-Binding ProteinsRNA FungalIron DeficienciesCell Biologybiology.organism_classificationDNA-Binding ProteinsRepressor ProteinsCheckpoint Kinase 2Protein SubunitsProtein TransportRibonucleotide reductaseBiochemistryCytoplasmTranscription Factors
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Yeast Dun1 Kinase Regulates Ribonucleotide Reductase Inhibitor Sml1 in Response to Iron Deficiency

2014

Iron is an essential micronutrient for all eukaryotic organisms because it participates as a redox-active cofactor in many biological processes, including DNA replication and repair. Eukaryotic ribonucleotide reductases (RNRs) are Fe-dependent enzymes that catalyze deoxyribonucleoside diphosphate (dNDP) synthesis. We show here that the levels of the Sml1 protein, a yeast RNR large-subunit inhibitor, specifically decrease in response to both nutritional and genetic Fe deficiencies in a Dun1-dependent but Mec1/Rad53- and Aft1-independent manner. The decline of Sml1 protein levels upon Fe starvation depends on Dun1 forkhead-associated and kinase domains, the 26S proteasome, and the vacuolar pr…

Iron-Sulfur ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleotideIronDeoxyribonucleotidesGenes FungalSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeRibonucleotide reductase inhibitorProtein Serine-Threonine KinasesBiologyProtein degradationchemistry.chemical_compoundTristetraprolinRibonucleotide ReductasesAspartic Acid EndopeptidasesPhosphorylationMolecular BiologyCheckpoint Kinase 2Binding SitesKinaseIntracellular Signaling Peptides and ProteinsArticlesCell Biologybiology.organism_classificationDNA-Binding ProteinsDeoxyribonucleosideCheckpoint Kinase 2chemistryBiochemistryProteolysisGene DeletionTranscription FactorsMolecular and Cellular Biology
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