Search results for "Protein Complex"

showing 10 items of 154 documents

A knowledge-based decision support system in bioinformatics: An application to protein complex extraction

2013

Abstract Background We introduce a Knowledge-based Decision Support System (KDSS) in order to face the Protein Complex Extraction issue. Using a Knowledge Base (KB) coding the expertise about the proposed scenario, our KDSS is able to suggest both strategies and tools, according to the features of input dataset. Our system provides a navigable workflow for the current experiment and furthermore it offers support in the configuration and running of every processing component of that workflow. This last feature makes our system a crossover between classical DSS and Workflow Management Systems. Results We briefly present the KDSS' architecture and basic concepts used in the design of the knowl…

Decision support systemSaccharomyces cerevisiae ProteinsComputer scienceKnowledge BasesCrossovercomputer.software_genreBioinformaticslcsh:Computer applications to medicine. Medical informaticsBiochemistryDecision Support TechniquesWorkflowSoftwareknowledge base; decision support systemStructural BiologyArtificial IntelligenceProtein Interaction MappingPreprocessorCluster analysisMolecular Biologylcsh:QH301-705.5Settore ING-INF/05 - Sistemi Di Elaborazione Delle Informazionibusiness.industryApplied MathematicsResearchComputational BiologyComputer Science ApplicationsWorkflowKnowledge baselcsh:Biology (General)Multiprotein Complexesprotein complex extractionlcsh:R858-859.7Data miningbusinesscomputerWorkflow management systemAlgorithmsSoftware
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Pulsed EPR determination of water accessibility to spin-labeled amino acid residues in LHCIIb.

2009

Membrane proteins reside in a structured environment in which some of their residues are accessible to water, some are in contact with alkyl chains of lipid molecules, and some are buried in the protein. Water accessibility of residues may change during folding or function-related structural dynamics. Several techniques based on the combination of pulsed electron paramagnetic resonance (EPR) with site-directed spin labeling can be used to quantify such water accessibility. Accessibility parameters for different residues in major plant light-harvesting complex IIb are determined by electron spin echo envelope modulation spectroscopy in the presence of deuterated water, deuterium contrast in …

DetergentsBiophysicsLight-Harvesting Protein ComplexesSpectroscopy Imaging and Other TechniquesBuffersCrystallography X-RaySpectral linelaw.inventionlawMoleculeHumansAmino AcidsElectron paramagnetic resonanceProtein Structure QuaternaryHyperfine structureAlkylPlant Proteinschemistry.chemical_classificationPulsed EPRChemistryElectron Spin Resonance SpectroscopyPeasTemperatureWaterSite-directed spin labelingCrystallographyDeuteriumSolubilityMutationSolventsSpin LabelsProtein MultimerizationBiophysical journal
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The importance of a highly active and DeltapH-regulated diatoxanthin epoxidase for the regulation of the PS II antenna function in diadinoxanthin cyc…

2005

The present study focuses on the regulation of diatoxanthin (Dtx) epoxidation in the diadinoxanthin (Ddx) cycle containing algae Phaeodactylum tricornutum, Thalassiosira pseudonana, Cyclotella meneghiniana and Prymnesium parvum and its significance for the control of the photosystem II (PS II) antenna function. Our data show that Dtx epoxidase can exhibit extremely high activities when algal cells are transferred from high light (HL) to low light (LL). Under HL conditions, Dtx epoxidation is strongly inhibited by the light-driven proton gradient. Uncoupling of the cells during HL illumination restores the high epoxidation rates observed during LL. In Ddx cycle containing algae, non-photoche…

DiatomsPhotosystem IIbiologyLightPhysiologyZeaxanthin epoxidaseAlgal ProteinsDiadinoxanthinDiatoxanthinEukaryotaPhotosystem II Protein ComplexPlant ScienceHydrogen-Ion ConcentrationXanthophyllsPhotochemistrychemistry.chemical_compoundchemistryPhotoprotectionbiology.proteinElectrochemical gradientChlorella vulgarisOxidoreductasesAgronomy and Crop ScienceChlorophyll fluorescenceViolaxanthinJournal of plant physiology
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The p21-activated kinase Mbt is a component of the apical protein complex in central brain neuroblasts and controls cell proliferation

2013

The final size of the central nervous system is determined by precisely controlled generation, proliferation and death of neural stem cells. We show here that the Drosophila PAK protein Mushroom bodies tiny (Mbt) is expressed in central brain progenitor cells (neuroblasts) and becomes enriched to the apical cortex of neuroblasts in a cell cycle- and Cdc42-dependent manner. Using mushroom body neuroblasts as a model system, we demonstrate that in the absence of Mbt function, neuroblasts and their progeny are correctly specified and are able to generate different neuron subclasses as in the wild type, but are impaired in their proliferation activity throughout development. In general, loss of…

Embryo Nonmammaliananimal structuresMitosisApoptosisCell CountSpindle ApparatusBiologyNeural Stem CellsNeuroblastGTP-Binding ProteinsTubulinCell polarityAnimalsDrosophila ProteinsProgenitor cellMolecular BiologyMitosisCell ProliferationCell SizeBinding SitesApical cortexAsymmetric Cell DivisionfungiBrainCell PolarityGene Expression Regulation DevelopmentalNeural stem cellCell biologyEnzyme ActivationActin CytoskeletonPhenotypenervous systemLarvaMultiprotein Complexesembryonic structuresMushroom bodiesDrosophilaProtein KinasesGanglion mother cellDevelopmental BiologyDevelopment
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Metabolic Adaptation and Protein Complexes in Prokaryotes.

2012

Protein complexes are classified and have been charted in several large-scale screening studies in prokaryotes. These complexes are organized in a factory-like fashion to optimize protein production and metabolism. Central components are conserved between different prokaryotes; major complexes involve carbohydrate, amino acid, fatty acid and nucleotide metabolism. Metabolic adaptation changes protein complexes according to environmental conditions. Protein modification depends on specific modifying enzymes. Proteins such as trigger enzymes display condition-dependent adaptation to different functions by participating in several complexes. Several bacterial pathogens adapt rapidly to intrace…

Endocrinology Diabetes and MetabolismMetaboliteSubstrate channelinglcsh:QR1-502ReviewBiologyBiochemistrylcsh:Microbiologyprokaryoteschemistry.chemical_compoundDownregulation and upregulationGene expressionProtein biosynthesisMolecular Biologymetaboliteschemistry.chemical_classificationprotein complexesE. coliMetabolismS. aureuschannelingAmino acidcrowdingEnzymechemistryBiochemistry
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γ2-Adaptin, a Ubiquitin-interacting Adaptor, Is a Substrate to Coupled Ubiquitination by the Ubiquitin Ligase Nedd4 and Functions in the Endosomal Pa…

2008

gamma2-Adaptin is a putative member of the clathrin adaptor protein family with unknown physiological function. We previously reported that gamma2-adaptin acts as a ubiquitin receptor by virtue of its ubiquitin-interacting motif. Here we demonstrate that this motif mediates a specific physical interaction with the ubiquitin ligase Nedd4 and promotes ubiquitination of gamma2-adaptin. By mapping regions of Nedd4 involved in binding to gamma2-adaptin, we identified its C2 domain to be essential, whereas the WW and HECT domains are dispensable. Consistent with this, we uncovered that the C2 domain of Nedd4 is ubiquitinated itself and as such is recruited by the ubiquitin-interacting motif of ga…

EndosomeNedd4 Ubiquitin Protein LigasesUbiquitin-Protein LigasesAmino Acid MotifsNEDD4Endosomesmacromolecular substancesUbiquitin-conjugating enzymeBiochemistryClathrinSubstrate SpecificityUbiquitinCell Line TumorHumansAdaptor Protein Complex gamma SubunitsMolecular BiologyC2 domainEndosomal Sorting Complexes Required for TransportEpidermal Growth FactorbiologyUbiquitinCell MembraneUbiquitinationSignal transducing adaptor proteinCell BiologyUbiquitin ligaseCell biologybiology.proteinProtein BindingJournal of Biological Chemistry
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γ2-Adaptin is functioning in the late endosomal sorting pathway and interacts with ESCRT-I and -III subunits.

2010

Abstractγ2-Adaptin is a clathrin adaptor-related protein with unclear physiological function. Previous studies indicated that γ2-adaptin might act within the multivesicular body (MVB) protein-sorting pathway that is central to receptor down-regulation, lysosome biogenesis, and budding of enveloped viruses. Here, we have analyzed the effects of excess and deficit γ2-adaptin on exogenous and endogenous MVB cargoes and on the MVB machinery itself. Foreign cargoes, like retroviral Gags, are entrapped by overexpressed γ2-adaptin in detergent-insoluble polymers and blocked in budding. When viral budding involves MVB/endosomal structures, excess γ2-adaptin acts by accelerating lysosomal Gag destru…

EndosomeViral buddingImmunoblottingGene Products gagmacromolecular substancesEndosomesTransfectionClathrinESCRTLysosomeCell Line TumormedicineBiomarkers TumorHumansMultivesicular bodyMultivesicular BodyMolecular BiologyAdaptor Protein Complex gamma SubunitsBuddingbiologyEndosomal Sorting Complexes Required for TransportCHMP2AVirus buddingMultivesicular BodiesVps28Cell BiologyLysosomeCell biologyLuminescent ProteinsProtein Transportmedicine.anatomical_structureRetroviridaeMicroscopy Fluorescencebiology.proteinRNA InterferenceLysosomesBiogenesisProtein BindingSignal TransductionBiochimica et biophysica acta
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Trafficking of the human transferrin receptor in plant cells: effects of tyrphostin A23 and brefeldin A.

2006

Plant cells possess much of the molecular machinery necessary for receptor-mediated endocytosis (RME), but this process still awaits detailed characterization. In order to identify a reliable and well-characterized marker to investigate RME in plant cells, we have expressed the human transferrin receptor (hTfR) in Arabidopsis protoplasts. We have found that hTfR is mainly found in endosomal (Ara7- and FM4-64-positive) compartments, but also at the plasma membrane, where it mediates binding and internalization of its natural ligand transferrin (Tfn). Cell surface expression of hTfR increases upon treatment with tyrphostin A23, which inhibits the interaction between the YTRF endocytosis signa…

Endosomemedia_common.quotation_subjectArabidopsisTransferrin receptorPlant ScienceBiologyEndocytosischemistry.chemical_compoundReceptors TransferrinGeneticsHumansEnzyme InhibitorsInternalizationmedia_commonchemistry.chemical_classificationProtein Synthesis InhibitorsBrefeldin AProtoplastsCell BiologyReceptor-mediated endocytosisBrefeldin ATyrphostinsPlants Genetically ModifiedCell biologyAdaptor Protein Complex mu SubunitsCytosolProtein TransportchemistryGene Expression RegulationTransferrinThe Plant journal : for cell and molecular biology
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Proteomic analysis of the photosystem I light-harvesting antenna in tomato (Lycopersicon esculentum).

2004

Until now, more genes of the light-harvesting antenna of higher-plant photosystem I (PSI) than proteins have been described. To improve our understanding of the composition of light-harvesting complex I (LHCI) of tomato (Lycopersicon esculentum), we combined one- and two-dimensional (1-D and 2-D, respectively) gel electrophoresis with immunoblotting and tandem mass spectrometry (MS/ MS). Separation of PSI with high-resolution 1-D gels allowed separation of five bands attributed to proteins of LHCI. Immunoblotting with monospecific antibodies and MS/MS analysis enabled the correct assignment of the four prominent bands to light-harvesting proteins Lhcal -4. The fifth band was recognized by o…

Gel electrophoresisGene isoformElectrophoresisProteomicsChromatographybiologyPhotosystem I Protein ComplexImmunoblottingMolecular Sequence DataLight-Harvesting Protein ComplexesContext (language use)Tandem mass spectrometrybiology.organism_classificationPhotosystem IBiochemistryLycopersiconMass SpectrometryIsoelectric pointBiochemistrySolanum lycopersicumSequence Analysis ProteinProtein IsoformsAmino Acid SequencePhotosystemBiochemistry
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Sorting of a secretory protein (gp80) to the apical surface of Caco-2 cells

1994

We have investigated the synthesis and polarized secretion of the exogenous gp80 glycoprotein complex in the human epithelial adenocarcinoma cell line, Caco-2. gp80 is secreted at the apical surface of Madin-Darby canine kidney (MDCK) cells and should, therefore, display the signal(s) required for sorting into the apical exocytic pathway. In Caco-2 cells, no bona fide secretory protein released preferentially at the apical surface has been described so far. To address the question of whether Caco-2 cells possess a machinery capable of delivery of secretory proteins at the apical surface, we stably transfected the cells with a recombinant gene coding for the gp80 glycoprotein complex. Pulse-…

Gene ExpressionBiologyTransfectionCell LineDogsGlycoprotein complexCell polarityTumor Cells CulturedAnimalsHumansSecretionchemistry.chemical_classificationMembrane GlycoproteinsCell MembraneCell PolarityCell BiologyTransfectionApical membraneReceptors Interleukin-6Molecular biologyCell biologyPhenotypeSecretory proteinchemistryCell cultureGlycoproteinJournal of Cell Science
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