Search results for " nucleus"

showing 10 items of 1270 documents

The DNA-binding subunit p140 of replication factor C is upregulated in cycling cells and associates with G 1 phase cell cycle regulatory proteins

1999

The DNA-binding subunit of replication factor C (RFCp140) plays an important role in both DNA replication and DNA repair. The mechanisms regulating activation of RFCp140 thereby controlling replication and cellular proliferation are largely unknown. We analyzed protein expression of RFCp140 during cell cycle progression and investigated the association of RFCp140 with cell cycle regulatory proteins in cell lines of various tissue origin and in primary hematopoietic cells. Western and Northern blot analyses of RFCp140 from synchronized cells showed downregulation of RFCp140 when cells enter a G0-like quiescent state and upregulation of RFCp140 in cycling cells. Translocation from the cytopla…

CytoplasmSaccharomyces cerevisiae ProteinsT-LymphocytesCyclin ACell Cycle ProteinsEukaryotic DNA replicationCell LineMinor Histocompatibility AntigensDNA replication factor CDT1MiceReplication factor CControl of chromosome duplicationDrug DiscoveryAnimalsHumansReplication Protein CGenetics (clinical)Cell NucleusHomeodomain ProteinsbiologyG1 PhaseS-phase-promoting factor3T3 CellsCell cycleMolecular biologyUp-RegulationCell biologyDNA-Binding ProteinsRepressor ProteinsProto-Oncogene Proteins c-bcl-2biology.proteinMolecular MedicineOrigin recognition complexJournal of Molecular Medicine
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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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Molecular basis of the functional distinction between Cln1 and Cln2 cyclins

2012

Cln1 and Cln2 are very similar but not identical cyclins. In this work, we tried to describe the molecular basis of the functional distinction between Cln1 and Cln2. We constructed chimeric cyclins containing different fragments of Cln1 and Cln2 and performed several functional analysis that make it possible to distinguish between Cln1 or Cln2. We identified that region between amino acids 225 and 299 of Cln2 is not only necessary but also sufficient to confer Cln2 specific functionality compared with Cln1. We also studied Cln1 and Cln2 subcellular localization identifying additional differences between them. Both cyclins are distributed between the nucleus and the cytoplasm, but Cln1 shows…

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticBlotting WesternGenes FungalGenetic VectorsGreen Fluorescent ProteinsActive Transport Cell NucleusSaccharomyces cerevisiaeKaryopherinsBiologyReportCyclinsGene Expression Regulation FungalmedicineAmino Acid SequenceNuclear export signalMolecular BiologyPeptide sequenceCyclinKaryopherinCell Nucleuschemistry.chemical_classificationCell Cycle CheckpointsCell BiologySubcellular localizationCell nucleusmedicine.anatomical_structureBiochemistrychemistryCytoplasmNuclear transportCDC28 Protein Kinase S cerevisiaePlasmidsDevelopmental BiologyCell Cycle
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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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Gene expression is circular: factors for mRNA degradation also foster mRNA synthesis.

2013

SummaryMaintaining proper mRNA levels is a key aspect in the regulation of gene expression. The balance between mRNA synthesis and decay determines these levels. We demonstrate that most yeast mRNAs are degraded by the cytoplasmic 5′-to-3′ pathway (the “decaysome”), as proposed previously. Unexpectedly, the level of these mRNAs is highly robust to perturbations in this major pathway because defects in various decaysome components lead to transcription downregulation. Moreover, these components shuttle between the cytoplasm and the nucleus, in a manner dependent on proper mRNA degradation. In the nucleus, they associate with chromatin—preferentially ∼30 bp upstream of transcription start-sit…

CytoplasmSaccharomyces cerevisiae ProteinsTranscription GeneticRNA StabilityGenes FungalRNA polymerase IIRNA-binding proteinSaccharomyces cerevisiaeGenètica molecularGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciencesGene Expression ProcessTranscription (biology)Gene Expression Regulation FungalGene expressionP-bodiesmedicineRNA Messenger030304 developmental biologyRegulation of gene expressionCell Nucleus0303 health sciencesbiologyBiochemistry Genetics and Molecular Biology(all)030302 biochemistry & molecular biologyRNA-Binding ProteinsRNA FungalMolecular biologyCell biologyCell nucleusmedicine.anatomical_structureExoribonucleasesbiology.proteinRNARNA Polymerase IICell
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Nuclear Translocation of Papillomavirus Minor Capsid Protein L2 Requires Hsc70

2004

ABSTRACT Minor capsid protein L2 of papillomaviruses plays an essential role in virus assembly by recruiting viral components to PML bodies, the proposed sites of virus morphogenesis. We demonstrate here that the function of L2 in virus assembly requires the chaperone Hsc70. Hsc70 was found dispersed in naturally infected keratinocytes and cultured cells. A dramatic relocation of Hsc70 from the cytoplasm to PML bodies was induced in these cells by L2 expression. Hsc70-L2 complex formation was confirmed by coimmunoprecipitation. The complex was modulated by the cochaperones Hip and Bag-1, which stabilize and destabilize Hsc70-substrate complexes, respectively. Cytoplasmic depletion of Hsc70 …

Cytoplasmanimal structuresImmunoprecipitationvirusesImmunologyActive Transport Cell Nucleusmacromolecular substancesBiologyMicrobiologyVirusGreen fluorescent proteinCell Line TumorVirologyAnimalsHSP70 Heat-Shock ProteinsCOS cellsHSC70 Heat-Shock ProteinsVirionOncogene Proteins ViralMolecular biologyVirus-Cell InteractionsTransport proteinCell biologyProtein TransportCapsidCytoplasmInsect ScienceChaperone (protein)COS Cellsembryonic structuresbiology.proteinCapsid ProteinsJournal of Virology
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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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Nuclear and Cytoplasmic Soluble Proteins Extraction from a Small Quantity of Drosophila’s Whole Larvae and Tissues

2015

The identification and study of protein’s function in several model organisms is carried out using both nuclear and cytoplasmic extracts. For a long time, Drosophila’s embryos have represented the main source for protein extractions, although in the last year, the importance of collecting proteins extracts also from larval tissues has also been understood. Here we report a very simple protocol, improved by a previously developed method, to produce in a single extraction both highly stable nuclear and cytoplasmic protein extracts from a small quantity of whole Drosophila’s larvae or tissues, suitable for biochemical analyses like co-immunoprecipitation.

Cytoplasmanimal structuresved/biology.organism_classification_rank.speciesBiologyCell FractionationCatalysislcsh:ChemistryInorganic ChemistryCytoplasmic proteinBotanyTechnical NoteAnimalsDrosophila ProteinsPhysical and Theoretical ChemistryModel organismlcsh:QH301-705.5Molecular BiologyDrosophilaSpectroscopyCell NucleusLarvaved/biologyOrganic ChemistryExtraction (chemistry)fungiproteins extractionEmbryoGeneral Medicinebiology.organism_classificationhnRNPsComputer Science ApplicationsDrosophila melanogasterlcsh:Biology (General)lcsh:QD1-999BiochemistryCytoplasmLarvaDrosophilaFunction (biology)International Journal of Molecular Sciences
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A comparison of cytoplasmic and nuclear estradiol and progesterone receptors in human fallopian tube and endometrial tissue

1981

Quantitative and qualitative aspects of the in vitro binding of 3 H-estradiol and 3 H-progesterone to receptor components from human endometrium and fallopian tube cytoplasmic and nuclear fractions were studied. The steroid binding macromolecules formed in vitro could be extracted from nuclei by 0.4M KCl and detected by glycerol gradient centrifugation. Both estradiol- and progesterone-binding compounds formed only one peak (under high ionic strength conditions) with a sedimentation coefficient of about 4-5S. The number of cytoplasmic and nuclear binding sites for both estradiol and R5020 varied dramatically throughout the menstrual cycle: the estradiol and progesterone receptor concentrati…

Cytoplasmmedicine.medical_specialtymedia_common.quotation_subjectmedicine.medical_treatmentBiologyPromegestoneSteroidInfundibulumEndometriumInternal medicineProgesterone receptorFollicular phasemedicineHumansTissue DistributionReceptorFallopian TubesProgesteroneMenstrual cyclemedia_commonCell NucleusEstradiolObstetrics and GynecologyMenstruationCytosolEndocrinologymedicine.anatomical_structureReceptors EstrogenReproductive MedicineFemaleReceptors Progesteronehormones hormone substitutes and hormone antagonistsFallopian tubeFertility and Sterility
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Activation of the human immune system via toll-like receptors by the oncolytic parvovirus H-1.

2012

This study aimed to investigate the function of toll-like receptors (TLRs) during oncolytic parvovirus H-1 (H-1PV)-induced human immune responses. First, the role of TLRs in the activation of the NFκB transcription factor was characterized; second, the immunologic effects of H-1PV-induced tumor cell lysates (TCL) on human antitumor immune responses were evaluated. A human ex vivo model was used to study immune responses with dendritic cells (DCs). Human embryonic kidney cells (HEK293) transfected to stably express TLRs were used as potential human DC equivalents to further investigate the role of specific TLRs during immune activation. TLR3 and TLR9 were activated by H-1PV infection, which …

Cytotoxicity ImmunologicH-1 parvovirusCancer ResearchCytoplasmParvovirus H-1chemical and pharmacologic phenomenaEnzyme-Linked Immunosorbent AssayBiologyKidneyProinflammatory cytokineParvoviridae InfectionsImmune systemTumor Cells CulturedHumansMelanomaCells CulturedCell NucleusOncolytic VirotherapyTumor Necrosis Factor-alphaToll-Like ReceptorsNF-kappa BDendritic CellsAcquired immune systemFlow CytometryCell biologyOncolytic virusOncolytic VirusesOncologyImmune SystemImmunologyTLR3CytokinesTumor necrosis factor alphaSignal transductionSignal TransductionInternational journal of cancer
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