Search results for "RNA-binding protein"

showing 10 items of 194 documents

Genetic manipulation of HSP26 and YHR087W stress genes may improve fermentative behaviour in wine yeasts under vinification conditions

2008

Throughout wine production yeast cells are affected by a plethora of stress conditions that compromise their ability to carry out the whole process. In recent years important knowledge about the mechanisms involved in stress response in both laboratory and wine yeast strains has been obtained. Several studies have indicated that a correlation exists between stress resistance, expression of stress response genes and fermentative behaviour. In this work we introduce several genetic manipulations in two genes induced by several stress conditions: HSP26 (which encodes a heat shock protein) and YHR087W (encoding a protein of unknown function) in two different wine yeasts, ICV16 and ICV27. These …

GeneticsWineSaccharomyces cerevisiae ProteinsTime FactorsSPI1CentromereRNA-Binding ProteinsWineSaccharomyces cerevisiaeGeneral MedicineBiologyMicrobiologyYeastYeast in winemakingPlasmidYeastsHeat shock proteinFermentationGene expressionPromoter Regions GeneticGeneHeat-Shock ProteinsPlasmidsFood ScienceInternational Journal of Food Microbiology
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Redox regulation of genome stability by effects on gene expression, epigenetic pathways and DNA damage/repair

2015

Reactive oxygen and nitrogen species (e.g. H2O2, nitric oxide) confer redox regulation of essential cellular signaling pathways such as cell differentiation, proliferation, migration and apoptosis. In addition, classical regulation of gene expression or activity, including gene transcription to RNA followed by translation to the protein level, by transcription factors (e.g. NF-κB, HIF-1α) and mRNA binding proteins (e.g. GAPDH, HuR) is subject to redox regulation. This review will give an update of recent discoveries in this field, and specifically highlight the impact of reactive oxygen and nitrogen species on DNA repair systems that contribute to genomic stability. Emphasis will be placed …

Genome instabilityRedox signalingRNA UntranslatedEpigenetic regulation of neurogenesisDNA RepairHuR mRNA-binding protein in the 3′-untranslated regionClinical BiochemistryHDAC histone deacetylaseReview ArticleAP-1 activator protein 1BiochemistryApe-1 apurinic/apyrimidinic endonuclease 1GPx-1 glutathione peroxidase-1Epigenesis GeneticHistonesTrx thioredoxinPHD prolylhydroxylaseBER base excision repairlcsh:QH301-705.5HO-1 heme oxygenase-1EpigenomicsGeneticsRegulation of gene expressionNox member of the NADPH oxidase familylcsh:R5-920JmjC Jumonji C domain-containing histone demethylasesHIF-1α hypoxia inducible factor-1α5-hmC 5-hydroxymethylcytosineddc:Cell biologyMMP matrix metalloproteinaseGrx glutaredoxinGAPDH glyceraldehyde-3-phosphate dehydrogenaseNrf2 nuclear factor erythroid related factor 2DNA methylationEpigeneticslcsh:Medicine (General)Oxidation-ReductionSignal Transduction5-mC 5-methylcytosineDNA repairDNA damageNF-κB nuclear factor-κBBiologyGenomic InstabilityRNS reactive nitrogen speciesROS reactive oxygen speciesNER nucleotide excision repairSOD superoxide dismutaseOxyR transcription factor (hydrogen peroxide-inducible genes activator)HumansEpigeneticsOrganic ChemistryPETN pentaerithrityl tetranitrateGene regulationOxidative StressDNMT DNA methyltransferaseGene Expression Regulationlcsh:Biology (General)AREs AU-rich elementsHAT histone acetyltransferaseKeap1 kelch-like ECH-associated protein 1BiomarkersCOPD chronic obstructive pulmonary disorderDNA DamageRedox Biology
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Genetic manipulation of longevity-related genes as a tool to regulate yeast life span and metabolite production during winemaking

2013

Abstract Background Yeast viability and vitality are essential for different industrial processes where the yeast Saccharomyces cerevisiae is used as a biotechnological tool. Therefore, the decline of yeast biological functions during aging may compromise their successful biotechnological use. Life span is controlled by a variety of molecular mechanisms, many of which are connected to stress tolerance and genomic stability, although the metabolic status of a cell has proven a main factor affecting its longevity. Acetic acid and ethanol accumulation shorten chronological life span (CLS), while glycerol extends it. Results Different age-related gene classes have been modified by deletion or o…

HST3GlycerolSaccharomyces cerevisiae ProteinsTranscription Genetic<it>HST3</it>Saccharomyces cerevisiaeLongevitylcsh:QR1-502SOD2BioengineeringApoptosisWinePUB1Saccharomyces cerevisiaeStressApplied Microbiology and Biotechnologylcsh:MicrobiologyHistone DeacetylasesStress granuleSirtuin 2<it>PUB1</it>Gene expressionChronological agingSirtuinsNADH NADPH OxidoreductasesRNA MessengerEthanol metabolismSilent Information Regulator Proteins Saccharomyces cerevisiaeAcetic AcidbiologyEthanolSuperoxide DismutaseResearchRNA-Binding Proteinsbiology.organism_classificationYeastYeastBiochemistryCaspasesFermentationMutationFermentationHistone deacetylaseGene DeletionBiotechnologyMicrobial Cell Factories
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Immunohistochemical Study as a Tool in Differential Diagnosis of Pediatric Malignant Rhabdoid Tumor

2010

Malignant rhabdoid tumors (MRTs) are aggressive childhood neoplasms, occurring mainly in the kidney and brain. We describe 2 unusual cases of extrarenal and noncranial location (liver and soft tissue with dissemination) mimicking hepatoblastoma, neuroblastoma or Ewing sarcoma. Both cases revealed a polyphenotypic profile, combined with cytokeratin, vimentin, and CD99 expression. INI1/BAF-47 showed negative protein nuclear expression in both cases, suggesting a diagnosis of MRT. An extensive immunohistochemical panel was performed to exclude pediatric tumors reminiscent of MRT. The genetic studies failed to detected MYCN amplification, 11q23 deletion, and EWS break-apart positivity. No alter…

HepatoblastomaPathologymedicine.medical_specialtySkin NeoplasmsHistologyDesmoplastic small-round-cell tumorChromosomal Proteins Non-HistoneCD9912E7 AntigenN-Myc Proto-Oncogene ProteinPathology and Forensic MedicineDiagnosis DifferentialNeoplasms Multiple PrimaryFatal OutcomeAntigens CDNeuroblastomaAntineoplastic Combined Chemotherapy ProtocolsmedicineHumansVimentinRhabdoid TumorChromosome AberrationsOncogene ProteinsN-Myc Proto-Oncogene Proteinbusiness.industryLiver NeoplasmsInfant NewbornInfantNuclear ProteinsWilms' tumorSMARCB1 Proteinmedicine.diseaseImmunohistochemistryDNA-Binding ProteinsMedical Laboratory TechnologyDrug Resistance NeoplasmKeratinsFemaleSarcomaRNA-Binding Protein EWSDifferential diagnosisbusinessCell Adhesion MoleculesTranscription FactorsApplied Immunohistochemistry &amp; Molecular Morphology
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Heterogeneous nuclear ribonucleoprotein (hnRNP) F is a novel component of oligodendroglial RNA transport granules contributing to regulation of myeli…

2011

Myelin basic protein (MBP) is a major component of central nervous system (CNS) myelin. The absence of MBP results in the loss of almost all compact myelin in the CNS. MBP mRNA is sorted into RNA granules that are transported to the periphery of oligodendrocytes in a translationally inactive state. A central mediator of this transport process is the trans-acting factor heterogeneous nuclear ribonucleoprotein (hnRNP) A2 that binds to the cis-acting A2-response element in the 3′UTR of MBP mRNA. Recently, we found that activation of the Src family nonreceptor tyrosine kinase Fyn in oligodendrocytes leads to phosphorylation of hnRNP A2 and to increased translation of MBP mRNA. Here, we identify…

Heterogeneous nuclear ribonucleoproteinRNA-binding proteinBiologyCytoplasmic GranulesProto-Oncogene Proteins c-fynBiochemistryenvironment and public healthMiceFYNNeurobiologyCompact myelinHeterogeneous-Nuclear Ribonucleoprotein Group A-BProtein biosynthesismedicineMRNA transportAnimalsHumansMolecular Biology3' Untranslated RegionsCells CulturedMyelin SheathHeterogeneous-Nuclear Ribonucleoprotein Group F-Hhemic and immune systemsBiological TransportMyelin Basic ProteinCell BiologyMolecular biologyOligodendrocyteMyelin basic proteinOligodendrogliamedicine.anatomical_structurenervous systemGene Expression Regulationembryonic structuresbiology.proteinbiological phenomena cell phenomena and immunityThe Journal of biological chemistry
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Identification in the rat brain of a set of nuclear proteins interacting with H1° mRNA

2012

Synthesis of H1° histone, in the developing rat brain, is also regulated at post-transcriptional level. Regulation of RNA metabolism depends on a series of RNA-binding proteins (RBPs); therefore, we searched for H1° mRNA-interacting proteins. With this aim, we used in vitro transcribed, biotinylated H1° RNA as bait to isolate, by a chromatographic approach, proteins which interact with this mRNA, in the nuclei of brain cells. Abundant RBPs, such as heterogeneous nuclear ribonucleoprotein (hnRNP) K and hnRNP A1, and molecular chaperones (heat shock cognate 70, Hsc70) were identified by mass spectrometry. Western blot analysis also revealed the presence of cold shock domain-containing protein…

Heterogeneous nuclear ribonucleoproteinRNA-binding proteinRNA-binding proteinBiologyenvironment and public healthHeterogeneous-Nuclear RibonucleoproteinsMass SpectrometryHistonesSettore BIO/10 - BiochimicaAnimalsRNA MessengerNuclear proteinRats WistarSettore BIO/06 - Anatomia Comparata E CitologiaRibonucleoproteinMessenger RNAPIPPinGeneral NeuroscienceRibonucleoprotein particleHSC70 Heat-Shock ProteinsRNABrainCSD-C2Molecular biologyCell biologyRatsHistonebiology.proteinH1° mRNAPost-transcriptional gene regulation
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Immunohistochemical detection of EWS and FLI-1 proteinss in Ewing sarcoma and primitive neuroectodermal tumors: comparative analysis with CD99 (MIC-2…

2001

The molecular analysis of the t(11;22) rearrangement involving EWS/FLI-1 genes is likely to be of diagnostic value in Ewing sarcoma (ES) and primitive neuroectodermal tumors (PNET). The objective of the current study was to analyze the immunohistochemical expression of the EWS and FLI-1 proteins in a group of small round-cell tumors (SRCT) to determine their specificity and relevance in their differential diagnosis. Forty-eight cases-10 conventional ES, 4 large-cell ES, 5 PNET, 9 neuroblastomas (NB), 6 undifferentiated synovial sarcomas (SS), 5 rhabdomyosarcomas (RB), 5 non-Hodgkin lymphomas (NHL), 1 round-cell liposarcoma, and 3 mesenchymal chondrosarcomas-were analyzed. Immunocytochemistr…

HistologyImmunocytochemistryCD99Sarcoma EwingLiposarcomaBiology12E7 AntigenSensitivity and SpecificityHeterogeneous-Nuclear RibonucleoproteinsPathology and Forensic Medicinechemistry.chemical_compoundAntigenAntigens CDProto-Oncogene ProteinsmedicineHumansNeuroectodermal Tumors PrimitiveProto-Oncogene Protein c-fli-1medicine.diseaseImmunohistochemistryDNA-Binding ProteinsMedical Laboratory TechnologyAntigen retrievalchemistryRibonucleoproteinsCancer researchTrans-ActivatorsImmunohistochemistrySarcomaDifferential diagnosisRNA-Binding Protein EWSCell Adhesion MoleculesApplied immunohistochemistrymolecular morphology : AIMM
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Suppression of CD8+ T cell recognition in the immediate-early phase of human cytomegalovirus infection.

2012

Human cytomegalovirus (HCMV) interferes with MHC class I-restricted antigen presentation and thereby reduces recognition by CD8+ T-cells. This interference is mediated primarily by endoplasmic reticulum-resident glycoproteins that are encoded in the US2–11 region of the viral genome. Such a suppression of recognition would be of particular importance immediately after infection, because several immunodominant viral antigens are already present in the cell in this phase. However, which of the evasion proteins gpUS2–11 interfere(s) with antigen presentation to CD8+ T-cells at this time of infection is not known. Here we address this question, using recombinant viruses (RV) that express only o…

Human cytomegalovirusVirulence FactorsvirusesAntigen presentationCytomegalovirusCD8-Positive T-LymphocytesCell LineImmune toleranceViral ProteinsViral Envelope ProteinsAntigenVirologyMHC class IImmune TolerancemedicineHumansCytotoxic T cellImmune EvasionbiologyHistocompatibility Antigens Class IRNA-Binding Proteinsvirus diseasesmedicine.diseaseVirologyCell cultureCytomegalovirus InfectionsImmunologybiology.proteinCD8
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Immune evasion proteins gpUS2 and gpUS11 of human cytomegalovirus incompletely protect infected cells from CD8 T cell recognition

2009

AbstractHuman cytomegalovirus (HCMV) encodes four glycoproteins, termed gpUS2, gpUS3, gpUS6 and gpUS11 that interfere with MHC class I biosynthesis and antigen presentation. Despite gpUS2–11 expression, however, HCMV infection is efficiently controlled by cytolytic CD8 T lymphocytes (CTL). To address the role of gpUS2 and gpUS11 in antigen presentation during viral infection, HCMV mutants were generated that expressed either gpUS2 or gpUS11 alone without coexpression of the three other proteins. Fibroblasts infected with these viruses showed reduced HLA-A2 and HLA-B7 surface expression. Surprisingly, however, CTL directed against the tegument protein pp65 and the regulatory IE1 protein stil…

Human cytomegalovirusvirusesAntigen presentationIE1CytomegalovirusCD8-Positive T-LymphocytesVirus ReplicationMajor histocompatibility complexpp65US2Immediate-Early ProteinsViral Matrix ProteinsHLA-B7 AntigenInterferon-gammaViral ProteinsImmune systemViral Envelope ProteinsVirologyHLA-A2 AntigenMHC class ImedicineHumansCytotoxic T cellCells CulturedAntigen PresentationbiologyImmune evasionRNA-Binding Proteinsvirus diseasesbiochemical phenomena metabolism and nutritionPhosphoproteinsmedicine.diseaseVirologyCTL*MutagenesisCTLCytomegalovirus InfectionsMHC class Ibiology.proteinUS11CD8Virology
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Post-translational modifications in the survival motor neuron protein

2004

Spinal muscular atrophy (SMA) is an autosomal recessive disease characterized by a progressive loss of the spinal motoneurons. The SMA-determining gene has been termed survival motor neuron (SMN) and is deleted or mutated in over 98% of patients. The encoded gene product is a protein expressed as different isoforms. In particular, we showed that the rat SMN cDNA produces two isoforms with Mr of 32 and 35 kDa, both localized in nuclear coiled bodies, but the 32 kDa form is also cytoplasmic, whereas the 35 kDa form is also microsomal. To determine the molecular relationship between these two isoforms and potential post-translational modifications, we performed transfection experiments with a …

INVOLVEMENTFORMSPRODUCTBiochemistryMiceChlorocebus aethiopsProtein IsoformsPhosphorylationCyclic AMP Response Element-Binding ProteinSMN PROTEINCells CulturedMotor NeuronsSPINAL MUSCULAR-ATROPHYRNA-Binding ProteinsSMN Complex Proteins3T3 CellsTransfectionmedicine.anatomical_structureSpinal CordCOS CellsSUBCELLULAR-LOCALIZATIONEXPRESSIONGene isoformRecombinant Fusion ProteinsBiophysicsNerve Tissue ProteinsBiologyMuscular Atrophy SpinalGene productSMN Complex ProteinsComplementary DNAmedicineAnimalsHumansMolecular BiologyCell BiologySpinal muscular atrophyMotor neuronmedicine.diseaseSurvival of Motor Neuron 1 ProteinMolecular biologyRatsnervous system diseasesMolecular WeightSEVERITYnervous systemBODIESProtein Processing Post-TranslationalDETERMINING GENEImmunostainingBiochemical and Biophysical Research Communications
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