Search results for "MUTATION"

showing 10 items of 2830 documents

The Yeast RNA Polymerase II-associated Factor Iwr1p Is Involved in the Basal and Regulated Transcription of Specific Genes

2009

RNA polymerase II (RNA pol II) is a multisubunit enzyme that requires many auxiliary factors for its activity. Over the years, these factors have been identified using both biochemical and genetic approaches. Recently, the systematic characterization of protein complexes by tandem affinity purification and mass spectroscopy has allowed the identification of new components of well established complexes, including the RNA pol II holoenzyme. Using this approach, a novel and highly conserved factor, Iwr1p, that physically interacts with most of the RNA pol II subunits has been described in yeast. Here we show that Iwr1p genetically interacts with components of the basal transcription machinery …

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticActive Transport Cell NucleusRNA polymerase IISaccharomyces cerevisiaeBiologyBiochemistryPhosphatesFungal ProteinsGene Expression Regulation FungalTranscription Chromatin and EpigeneticsPromoter Regions GeneticMolecular BiologyRNA polymerase II holoenzymeGeneticsModels Geneticbeta-FructofuranosidaseGeneral transcription factorCell BiologyCell biologyKineticsGene Expression RegulationMicroscopy FluorescenceMutationbiology.proteinTranscription factor II FRNA Polymerase IITranscription factor II ETranscription factor II DCarrier ProteinsTranscription factor II BTranscription factor II AJournal of Biological Chemistry
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Cell Cycle Activation of the Swi6p Transcription Factor Is Linked to Nucleocytoplasmic Shuttling

2003

The control of the subcellular localization of cell cycle regulators has emerged as a crucial mechanism in the regulation of cell division. In the present work, we have characterized the function of the karyopherin Msn5p in the control of the cell cycle of Saccharomyces cerevisiae. Phenotypic analysis of the msn5 mutant revealed an increase in cell size and a functional interaction between Msn5p and the cell cycle transcription factor SBF (composed of the Swi4p and Swi6p proteins), indicating that Msn5p is involved in Start control. In fact, we have shown that the level of Cln2p protein is drastically reduced in an msn5 mutant. The effect on CLN2 expression is mediated at a transcriptional …

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticCell divisionChromosomal Proteins Non-HistoneActive Transport Cell NucleusSaccharomyces cerevisiaeKaryopherinsBiologyDNA-binding proteinCyclinsGene Expression Regulation FungalmedicineCell Growth and DevelopmentMolecular BiologyTranscription factorKaryopherinCell Nucleuschemistry.chemical_classificationCell CycleCell BiologyCell cycleSubcellular localizationCell biologyDNA-Binding ProteinsCell nucleusmedicine.anatomical_structurechemistryCytoplasmMutationCarrier ProteinsTranscription FactorsMolecular and Cellular Biology
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A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase

1999

Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser231 residue, located within the KIM. Upon phosphorylation of Ser231, PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal–regulated kinase (ERK)1/2 and p38α were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Cα catalytic subunit …

Cytoplasmanimal structuresRecombinant Fusion ProteinsCèl·lulesAmino Acid MotifsNerve Tissue ProteinsProtein tyrosine phosphataseSH2 domainTransfectionenvironment and public healthModels Biologicalp38 Mitogen-Activated Protein KinasesReceptor tyrosine kinaseSH3 domainCell LinePhosphoserinetyrosine phosphatasesAnimalsHumansProtein phosphorylationPKAReceptor-Like Protein Tyrosine Phosphatases Class 7PhosphorylationPTP-SLCell NucleusMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3biologyBrief ReportIntracellular Signaling Peptides and ProteinsBiological TransportCell BiologyProtein Tyrosine Phosphatases Non-ReceptorCyclic AMP-Dependent Protein KinasesEnzyme Activationenzymes and coenzymes (carbohydrates)MAP kinasesBiochemistryMitogen-activated protein kinaseCOS CellsMutationbiology.proteinPhosphorylationMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesEnzimssignal transductionProto-oncogene tyrosine-protein kinase Src
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The sequence alteration associated with a mutational hotspot in p53 protects cells from lysis by cytotoxic T lymphocytes specific for a flanking pept…

1998

A high proportion of tumors arise due to mutation of the p53 tumor suppressor protein. A p53 hotspot mutation at amino acid position 273 from R to H, flanking a peptide epitope that spans residues 264–272, renders cells resistant to killing by human histocompatibility leukocyte antigen (HLA)-A*0201–restricted cytotoxic T lymphocytes (CTLs) specific for this epitope. Acquisition of the R to H mutation at residue 273 of the human p53 protein promotes tumor growth in vivo by selective escape from recognition by p53.264–272 peptide-specific CTLs. Synthetic 27-mer p53 polypeptides covering the antigenic nonamer region 264–272 of p53 were used as proteasome substrates to investigate whether the R…

Cytotoxicity Immunologicp53Epitopes T-LymphocyteEpitopeSubstrate SpecificityMice0302 clinical medicineTumor Cells CulturedImmunology and AllergyCytotoxic T cellPeptide sequence0303 health sciencesAntigen PresentationproteasomesHydrolysisArticles3. Good healthCysteine Endopeptidasestumor antigensCell DivisionProteasome Endopeptidase ComplexImmunologyAntigen presentationMolecular Sequence DataMice TransgenicBiologyArgininecytotoxic T lymphocytes03 medical and health sciencesAntigenMultienzyme Complexesantigen processingAnimalsHumansPoint MutationHistidineAmino Acid Sequence030304 developmental biologyBinding SitesLinear epitopeHLA-A AntigensPoint mutationCytotoxicity Tests ImmunologicMolecular biologyPeptide FragmentsCTL*Tumor Suppressor Protein p53Peptides030215 immunologyT-Lymphocytes CytotoxicThe Journal of experimental medicine
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Using Y-chromosome capture enrichment to resolve haplogroup H2 shows new evidence for a two-path Neolithic expansion to Western Europe

2021

Uniparentally-inherited markers on mitochondrial DNA (mtDNA) and the non-recombining regions of the Y chromosome (NRY), have been used for the past 30 years to investigate the history of humans from a maternal and paternal perspective. Researchers have preferred mtDNA due to its abundance in the cells, and comparatively high substitution rate. Conversely, the NRY is less susceptible to back mutations and saturation, and is potentially more informative than mtDNA owing to its longer sequence length. However, due to comparatively poor NRY coverage via shotgun sequencing, and the relatively low and biased representation of Y-chromosome variants on capture assays such as the 1240 k, ancient DNA…

CzechSELECTIONPopulation geneticsMITOCHONDRIAL-DNAearly farmersDIVERSITYmitochondrial DNAshotgun sequencingPrehistòriaHaplogroupGerman0302 clinical medicineMedicine and Health SciencesDNA sequencingScience and technologymedia_common0303 health sciencesMultidisciplinaryHorizon (archaeology)Critical eventShotgun sequencingchromosomal haplogroupsEuropean researchQRSTEPPEWestern europelanguageMedicineGenetic MarkersMitochondrial DNA[SHS.ARCHEO]Humanities and Social Sciences/Archaeology and Prehistoryuniparentally-inherited markersScienceLibrary scienceBiologyY chromosomeDNA MitochondrialPolymorphism Single NucleotideTarget enrichmentArticle03 medical and health sciencesPolitical scienceHumansmedia_common.cataloged_instanceANCIENT DNAGenetic TestingEuropean unionAlleles030304 developmental biologyMUTATION-RATEChromosomes Human YY chromosomeSaturation (genetic)History and ArchaeologyY-mappable capture assayAncient DNA; Neanderthals; Anatomically modern humanslanguage.human_languageNeolithic transitionGenetics PopulationAncient DNAHaplotypesEvolutionary biologyGENOMIC HISTORY030217 neurology & neurosurgery
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Compromised repair of radiation-induced DNA double-strand breaks in Fanconi anemia fibroblasts in G2

2020

Fanconi anemia (FA) is a rare chromosomal instability syndrome with various clinical features and high cancer incidence. Despite being a DNA repair disorder syndrome and a frequently observed clinical hypersensitivity of FA patients towards ionizing radiation, the experimental evidence regarding the efficiency of radiation-induced DNA double-strand break (DSB) repair in FA is very controversial. Here, we performed a thorough analysis of the repair of radiation-induced DSBs in G1 and G2 in FA fibroblasts of complementation groups A, C, D1 (BRCA2), D2, E, F, G and P (SLX4) in comparison to normal human lung and skin fibroblasts. γH2AX, 53BP1, or RPA foci quantification after X-irradiation was…

DNA End-Joining RepairBiologyBiochemistryFanconi Anemia Complementation Group F ProteinHistonesRecombinases03 medical and health scienceschemistry.chemical_compound0302 clinical medicineFanconi anemiaChromosome instabilitymedicineHumansDNA Breaks Double-StrandedFanconi Anemia Complementation Group G ProteinMolecular BiologyCells Cultured030304 developmental biologyBRCA2 ProteinChromosome Aberrations0303 health sciencesFanconi Anemia Complementation Group A ProteinFanconi Anemia Complementation Group D2 ProteinX-RaysCell CycleFanconi Anemia Complementation Group C ProteinRecombinational DNA RepairChromosomeDNACell BiologyFibroblastsCell cyclemedicine.diseaseFanconi Anemia Complementation Group E ProteinComplementationKineticsenzymes and coenzymes (carbohydrates)Fanconi Anemiachemistry030220 oncology & carcinogenesisPremature chromosome condensationMutationCancer researchChromatidTumor Suppressor p53-Binding Protein 1DNADNA Repair
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Preservation of genetic and regulatory robustness in ancient gene duplicates of Saccharomyces cerevisiae

2014

[EN] Biological systems remain robust against certain genetic and environmental challenges. Robustness allows the exploration of ecological adaptations. It is unclear what factors contribute to increasing robustness. Gene duplication has been considered to increase genetic robustness through functional redundancy, accelerating the evolution of novel functions. However, recent findings have questioned the link between duplication and robustness. In particular, it remains elusive whether ancient duplicates still bear potential for innovation through preserved redundancy and robustness. Here we have investigated this question by evolving the yeast Saccharomyces cerevisiae for 2200 generations …

DNA Mutational AnalysisGenes FungalSaccharomyces cerevisiaeSaccharomyces cerevisiaeBiologyPolymorphism Single NucleotideGenome03 medical and health sciences0302 clinical medicineINDEL MutationStress PhysiologicalGene DuplicationGene duplicationDNA Mutational AnalysisGeneticsBiologyGeneGenetics (clinical)030304 developmental biologyGenetics0303 health sciencesModels GeneticResearchFungal geneticsRobustness (evolution)biology.organism_classificationAdaptation PhysiologicalPhenotypeEvolutionary biologyMutationChromosomes FungalDirected Molecular EvolutionGenome FungalAlgorithms030217 neurology & neurosurgeryGenome Research
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Deinococcus radiodurans' SRA-HNH domain containing protein Shp (Dr1533) is involved in faithful genome inheritance maintenance following DNA damage

2018

WOS:000452343100012; International audience; Background: Deinococcus radiodurans R1 (DR) survives conditions of extreme desiccation, irradiation and exposure to genotoxic chemicals, due to efficient DNA breaks repair, also through Mn2+ protection of DNA repair enzymes. Methods: Possible annotated domains of the DR1533 locus protein (Shp) were searched by bioinformatic analysis. The gene was cloned and expressed as fusion protein. Band-shift assays of Shp or the SRA and HNH domains were performed on oligonucleotides, genomic DNA from E. coif and DR. slip knock-out mutant was generated by homologous recombination with a kanamycin resistance cassette. Results: DR1533 contains an N-terminal SRA…

DNA RepairDNA cytosine-methylation; DNA damage; DR1533 locus; Genotoxic agents; Mn2+; SRA domain; Biophysics; Biochemistry; Molecular BiologyGenotoxic agents[SDV]Life Sciences [q-bio]DNA cytosine-methylationperspectiveSettore BIO/19 - Microbiologia GeneraleBiochemistrychemistry.chemical_compound0302 clinical medicineKanamycinCloning Molecularcytosine0303 health sciencesDR1533 locusbiologyChemistryGenotoxic agentuhrf1Mn(2+)Mn2+SRA domainDeinococcusrecognitionmanganese(ii)DNA BacterialDNA damageDNA repairoxidationUbiquitin-Protein LigasesBiophysicsSettore BIO/11 - Biologia Molecolareresistance03 medical and health sciencesBacterial ProteinsProtein DomainsDR1533 locuDrug Resistance BacterialEscherichia coliHumansfeaturesAmino Acid SequenceGeneMolecular Biology030304 developmental biologyOligonucleotideComputational BiologyDeinococcus radioduransDNA Methylationbiology.organism_classificationMolecular biologygenomic DNArepairMutationCCAAT-Enhancer-Binding ProteinsDNA damageHomologous recombination030217 neurology & neurosurgeryDNAGenome BacterialMutagens
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Targeting components of the alternative NHEJ pathway sensitizes KRAS mutant leukemic cells to chemotherapy.

2014

Abstract Activating KRAS mutations are detected in a substantial number of hematologic malignancies. In a murine T-cell acute lymphoblastic leukemia (T-ALL) model, we previously showed that expression of oncogenic Kras induced a premalignant state accompanied with an arrest in T-cell differentiation and acquisition of somatic Notch1 mutations. These findings prompted us to investigate whether the expression of oncogenic KRAS directly affects DNA damage repair. Applying divergent, but complementary, genetic approaches, we demonstrate that the expression of KRAS mutants is associated with increased expression of DNA ligase 3α, poly(ADP-ribose) polymerase 1 (PARP1), and X-ray repair cross-comp…

DNA RepairImmunologyAntineoplastic AgentsApoptosisMice TransgenicBiologymedicine.disease_causePrecursor T-Cell Lymphoblastic Leukemia-LymphomaBiochemistryProto-Oncogene Proteins p21(ras)chemistry.chemical_compoundXRCC1MicePARP1Transduction GeneticmedicineAnimalsHumansDNA Breaks Double-Strandedchemistry.chemical_classificationGeneticsDNA ligaseMutationGene knockdownCell BiologyHematologyImmunohistochemistryComet assayMice Inbred C57BLDisease Models AnimalchemistryMutationCancer researchKRASComet AssayDNABlood
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Nucleotide excision repair of abasic DNA lesions

2019

AbstractApurinic/apyrimidinic (AP) sites are a class of highly mutagenic and toxic DNA lesions arising in the genome from a number of exogenous and endogenous sources. Repair of AP lesions takes place predominantly by the base excision pathway (BER). However, among chemically heterogeneous AP lesions formed in DNA, some are resistant to the endonuclease APE1 and thus refractory to BER. Here, we employed two types of reporter constructs accommodating synthetic APE1-resistant AP lesions to investigate the auxiliary repair mechanisms in human cells. By combined analyses of recovery of the transcription rate and suppression of transcriptional mutagenesis at specifically positioned AP lesions, w…

DNA RepairTranscription GeneticDNA damageDNA repairGenome Integrity Repair and ReplicationGene Knockout Techniques03 medical and health sciencesEndonucleasechemistry.chemical_compoundTranscription (biology)CRISPR-Associated Protein 9DNA-(Apurinic or Apyrimidinic Site) LyaseGeneticsHumansAP siteCell Line TransformedSkin030304 developmental biologyGene Editing0303 health sciencesBase SequencebiologyGenome Human030302 biochemistry & molecular biologyDNABase excision repairFibroblastsMolecular biologyXeroderma Pigmentosum Group A ProteinDNA-Binding ProteinschemistryMutationbiology.proteinCRISPR-Cas SystemsDNADNA DamageProtein BindingNucleotide excision repairNucleic Acids Research
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