0000000000448148

AUTHOR

Natalia Gomez-navarro

showing 5 related works from this author

Defects in the NC2 repressor affect both canonical and non-coding RNA polymerase II transcription initiation in yeast.

2016

BACKGROUND: The formation of the pre-initiation complex in eukaryotic genes is a key step in transcription initiation. The TATA-binding protein (TBP) is a universal component of all pre-initiation complexes for all kinds of RNA polymerase II (RNA pol II) genes, including those with a TATA or a TATA-like element, both those that encode proteins and those that transcribe non-coding RNAs. Mot1 and the negative cofactor 2 (NC2) complex are regulators of TBP, and it has been shown that depletion of these factors in yeast leads to defects in the control of transcription initiation that alter cryptic transcription levels in selected yeast loci. RESULTS: In order to cast light on the molecular func…

0301 basic medicineSaccharomyces cerevisiae ProteinsTranscription GeneticRNA polymerase IISaccharomyces cerevisiaeGenètica molecularNC203 medical and health sciencesSaccharomycesTranscripció genèticaGeneticsTATACryptic transcriptRNA polymerase II holoenzymeGeneticsbiologyGeneral transcription factorTATA-Box Binding ProteinTranscription initiationPhosphoproteinsTATA-Box Binding ProteinYeastRepressor Proteins030104 developmental biologyTATA-likebiology.proteinTranscription factor II FATP-Binding Cassette TransportersRNA Polymerase IITranscription factor II DTranscriptomeTranscription factor II BProteïnesTranscription factor II AResearch ArticleBiotechnologyTranscription Factors
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Different pathways for the nuclear import of yeast RNA polymerase II

2015

Recent studies suggest that RNA polymerase II (Pol II) has to be fully assembled before being imported into the nucleus, while other reports indicate a distinct mechanism to import large and small subunits. In yeast, Iwr1 binds to the holoenzyme assembled in the cytoplasm and directs its nuclear entry. However, as IWR1 is not an essential gene, Iwr1-independent pathway(s) for the nuclear import of Pol II must exist. In this paper, we investigate the transport into the nucleus of several large and small Pol II subunits in the mutants of genes involved in Pol II biogenesis. We also analyse subcellular localization in the presence of drugs that can potentially affect Pol II nuclear import. Our…

Active Transport Cell NucleusBiophysicsRNA polymerase IISaccharomyces cerevisiaeBiochemistrychemistry.chemical_compoundStructural BiologyRNA polymeraseGeneticsmedicineMolecular BiologyCell NucleusbiologyProcessivitySubcellular localizationMolecular biologyCell biologyCell nucleusmedicine.anatomical_structurechemistrybiology.proteinRNA Polymerase IITranscription factor II DNuclear transportCarrier ProteinsBiogenesisBiochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
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Iwr1 facilitates RNA polymerase II dynamics during transcription elongation.

2017

Iwr1 is an RNA polymerase II (RNPII) interacting protein that directs nuclear import of the enzyme which has been previously assembled in the cytoplasm. Here we present genetic and molecular evidence that links Iwr1 with transcription. Our results indicate that Iwr1 interacts with RNPII during elongation and is involved in the disassembly of the enzyme from chromatin. This function is especially important in resolving problems posed by damage-arrested RNPII, as shown by the sensitivity of iwr1 mutants to genotoxic drugs and the Iwr1's genetic interactions with RNPII degradation pathway mutants. Moreover, absence of Iwr1 causes genome instability that is enhanced by defects in the DNA repair…

0301 basic medicineTranscription factoriesCytoplasmSaccharomyces cerevisiae ProteinsDNA RepairTranscription GeneticBiophysicsActive Transport Cell NucleusRNA polymerase IISaccharomyces cerevisiaeBiochemistryGenomic Instability03 medical and health sciencesStructural BiologyGeneticsMolecular BiologyRNA polymerase II holoenzymePolymeraseCell NucleusbiologyGeneral transcription factorMolecular biologyChromatinCell biology030104 developmental biologybiology.proteinTranscription factor II FRNA Polymerase IITranscription factor II DCarrier ProteinsTranscription factor II BDNA DamageBiochimica et biophysica acta. Gene regulatory mechanisms
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Insights into mRNP biogenesis provided by new genetic interactions among export and transcription factors.

2012

Abstract Background The various steps of mRNP biogenesis (transcription, processing and export) are interconnected. It has been shown that the transcription machinery plays a pivotal role in mRNP assembly, since several mRNA export factors are recruited during transcription and physically interact with components of the transcription machinery. Although the shuttling DEAD-box protein Dbp5p is concentrated on the cytoplasmic fibrils of the NPC, previous studies demonstrated that it interacts physically and genetically with factors involved in transcription initiation. Results We investigated the effect of mutations affecting various components of the transcription initiation apparatus on the…

Nucleocytoplasmic Transport ProteinsSaccharomyces cerevisiae Proteinslcsh:QH426-470MutantActive Transport Cell NucleusRNA-binding proteinRNA polymerase IISaccharomyces cerevisiaeDEAD-box RNA HelicasesTranscription (biology)GeneticsGenetics(clinical)RNA MessengerNuclear poreMex67pTranscription factorGenetics (clinical)AllelesDbp5pGeneticsmRNA exportbiologyGeneral transcription factorfungiNuclear ProteinsRNA-Binding Proteinslcsh:GeneticsRibonucleoproteinsMutationbiology.proteinNuclear PoreRNA Polymerase IINuclear Pore ComplexTranscriptionBiogenesisTranscription FactorsResearch ArticleBMC genetics
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Rtp1p Is a Karyopherin-Like Protein Required for RNA Polymerase II Biogenesis

2013

The assembly and nuclear transport of RNA polymerase II (RNA pol II) are processes that require the participation of many auxiliary factors. In a yeast genetic screen, we identified a previously uncharacterized gene, YMR185w (renamed RTP1), which encodes a protein required for the nuclear import of RNA pol II. Using protein affinity purification coupled to mass spectrometry, we identified interactions between Rtp1p and members of the R2TP complex. Rtp1p also interacts, to a different extent, with several RNA pol II subunits. The pattern of interactions is compatible with a role for Rtp1p as an assembly factor that participates in the formation of the Rpb2/Rpb3 subassembly complex and its bi…

Saccharomyces cerevisiae ProteinsActive Transport Cell NucleusRNA polymerase IISaccharomyces cerevisiaeKaryopherinsBiologyGene Expression Regulation FungalTranscriptional regulationRNA polymerase IProtein Interaction MapsMolecular BiologyRNA polymerase II holoenzymeR2TP complexGeneticsNuclear cap-binding protein complexArticlesCell BiologyPhosphoproteinsUp-RegulationCell biologyNuclear Pore Complex Proteinsbiology.proteinRNA Polymerase IITranscription factor II DCarrier ProteinsGene DeletionSmall nuclear RNATranscription Factors
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