Search results for "Protein Complex"

showing 10 items of 154 documents

Structural stability and properties of three isoforms of the major light-harvesting chlorophyll a/b complexes of photosystem II.

2008

AbstractThree isoforms of the major light-harvesting chlorophyll (Chl) a/b complexs of photosystem II (LHCIIb) in the pea, namely, Lhcb1, Lhcb2, and Lhcb3, were obtained by overexpression of apoprotein in Escherichia coli and by successfully refolding these isoforms with thylakoid pigments in vitro. The sequences of the protein, pigment stoichiometries, spectroscopic characteristics, thermo- and photostabilities of different isoforms were analysed. Comparison of their spectroscopic properties and structural stabilities revealed that Lhcb3 differed strongly from Lhcb1 and Lhcb2 in both respects. It showed the lowest Qy transition energy, with its reddest absorption about 2 nm red-shifted, an…

Gene isoformChlorophyllChlorophyll aProtein FoldingPhotosystem IIBiophysicsLight-Harvesting Protein ComplexesPhotochemistryBiochemistryThylakoidsReconstitutionchemistry.chemical_compoundPigmentPigment stoichiometryEscherichia coliThermal stabilityMajor light-harvesting chlorophyll a/b complex of photosystem IIProtein Structure QuaternaryThermostabilityPlant ProteinsChlorophyll APeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsIsoenzymeschemistryPhotostabilityChlorophyllThylakoidvisual_artBiophysicsvisual_art.visual_art_mediumThermostabilityBiochimica et biophysica acta
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Usher syndrome: molecular links of pathogenesis, proteins and pathways.

2006

Contains fulltext : 50437.pdf (Publisher’s version ) (Closed access) Usher syndrome is the most common form of deaf-blindness. The syndrome is both clinically and genetically heterogeneous, and to date, eight causative genes have been identified. The proteins encoded by these genes are part of a dynamic protein complex that is present in hair cells of the inner ear and in photoreceptor cells of the retina. The localization of the Usher proteins and the phenotype in animal models indicate that the Usher protein complex is essential in the morphogenesis of the stereocilia bundle in hair cells and in the calycal processes of photoreceptor cells. In addition, the Usher proteins are important in…

Genetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeCell Cycle ProteinsNerve Tissue ProteinsBiologyRetinaAdherens junctionMiceHair Cells AuditoryCell polarityGeneticsmedicineotorhinolaryngologic diseasesNeurosensory disorders [UMCN 3.3]AnimalsHumansProtein IsoformsCell Cycle ProteinMolecular BiologyGenetics (clinical)Renal disorder [IGMD 9]Adaptor Proteins Signal TransducingStereociliumMembrane ProteinsSignal transducing adaptor proteinGeneral MedicineActin cytoskeletonmedicine.diseaseeye diseasesCell biologyCytoskeletal ProteinsGenetic defects of metabolism [UMCN 5.1]Ear InnerMultiprotein ComplexesCateninSynapsessense organsUsher SyndromesPhotoreceptor Cells Vertebrate
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Retention mechanisms for ER and Golgi membrane proteins

2014

Unless there are mechanisms to selectively retain membrane proteins in the endoplasmic reticulum (ER) or in the Golgi apparatus, they automatically proceed downstream to the plasma or vacuole membranes. Two types of coat protein complex I (COPI)-interacting motifs in the cytosolic tails of membrane proteins seem to facilitate membrane retention in the early secretory pathway of plants: a dilysine (KKXX) motif (which is typical of p24 proteins) for the ER and a KXE/D motif (which occurs in the Arabidopsis endomembrane protein EMP12) for the Golgi apparatus. The KXE/D motif is highly conserved in all eukaryotic EMPs and is additionally present in hundreds of other proteins of unknown subcellu…

Golgi membraneSecretory PathwayKKXXMolecular Sequence DataGolgi ApparatusMembrane ProteinsGolgi TargetingPlant ScienceCOPIGolgi apparatusBiologyEndoplasmic ReticulumCoat Protein Complex ICell biologysymbols.namesakeMembrane proteinPlant CellssymbolsAmino Acid SequenceIntegral membrane proteinSecretory pathwayTrends in Plant Science
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The aryl hydrocarbon receptor-dependent deregulation of cell cycle control induced by polycyclic aromatic hydrocarbons in rat liver epithelial cells

2006

Disruption of cell proliferation control by polycyclic aromatic hydrocarbons (PAHs) may contribute to their carcinogenicity. We investigated role of the aryl hydrocarbon receptor (AhR) in disruption of contact inhibition in rat liver epithelial WB-F344 'stem-like' cells, induced by the weakly mutagenic benz[a]anthracene (BaA), benzo[b]fluoranthene (BbF) and by the strongly mutagenic benzo[a]pyrene (BaP). There were significant differences between the effects of BaA and BbF, and those of the strongly genotoxic BaP. Both BaA and BbF increased percentage of cells entering S-phase and cell numbers, associated with an increased expression of Cyclin A and Cyclin A/cdk2 complex activity. Their eff…

Health Toxicology and MutagenesisCyclin AGene ExpressionApoptosisCell Cycle ProteinsCyclin ACell LineBenz(a)AnthracenesBenzo(a)pyreneCytochrome P-450 CYP1A1polycyclic compoundsGeneticsAnimalsRat liver ‘stem-like’ cellsRNA MessengerPolycyclic Aromatic HydrocarbonsRNA Small InterferingMolecular BiologyAryl hydrocarbon receptorCell proliferationCarcinogenCell ProliferationFluorenesBase SequencebiologyChemistryCell growthCell CycleCyclin-Dependent Kinase 2Contact inhibitionEpithelial CellsTransfectionAryl hydrocarbon receptorMolecular biologyPolycyclic aromatic hydrocarbonsPolycyclic Hydrocarbons AromaticRatsReceptors Aryl HydrocarbonBiochemistryApoptosisMultiprotein ComplexesContact inhibitionMutationHepatocytesbiology.proteinCDK inhibitorMutagensMutation Research/Fundamental and Molecular Mechanisms of Mutagenesis
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Hepatitis B virus maturation is sensitive to functional inhibition of ESCRT-III, Vps4, and gamma 2-adaptin.

2007

ABSTRACT Hepatitis B virus (HBV) is an enveloped DNA virus that presumably buds at intracellular membranes of infected cells. HBV budding involves two endocytic host proteins, the ubiquitin-interacting adaptor γ2-adaptin and the Nedd4 ubiquitin ligase. Here, we demonstrate that HBV release also requires the cellular machinery that generates internal vesicles of multivesicular bodies (MVBs). In order to perturb the MVB machinery in HBV-replicating liver cells, we used ectopic expression of dominant-negative mutants of different MVB components, like the ESCRT-III complex-forming CHMP proteins and the Vps4 ATPases. Upon coexpression of mutated CHMP3, CHMP4B, or CHMP4C forms, as well as of ATPa…

Hepatitis B virusVacuolar Proton-Translocating ATPasesEndosomeImmunologyEndocytic cycleVesicular Transport Proteinsmacromolecular substancesEndosomesmedicine.disease_causeMicrobiologyESCRTVirusCell LineViral ProteinsVirologymedicineHumansAdaptor Protein Complex gamma SubunitsHepatitis B virusAdenosine TriphosphatasesMicroscopy ConfocalbiologyEndosomal Sorting Complexes Required for TransportVirus AssemblyDNA virusMolecular biologyUbiquitin ligaseCell biologyGenome Replication and Regulation of Viral Gene ExpressionMicroscopy FluorescenceInsect Sciencebiology.proteinHepatocytesATPases Associated with Diverse Cellular ActivitiesEctopic expressionJournal of virology
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Hepatitis B Virus Large Envelope Protein Interacts with γ2-Adaptin, a Clathrin Adaptor-Related Protein

2001

ABSTRACT For the outcome of a hepatitis B virus (HBV) infection, the viral L envelope protein with its pre-S domain performs pivotal functions by mediating attachment of HBV to liver cells, envelopment of viral capsids, release of (sub)viral particles, regulation of supercoiled DNA amplification, and transcriptional transactivation. To assess its multiple functions and host-protein assistance involved, we initiated a two-hybrid screen using the L-specific pre-S1 domain as bait. With this approach, we have identified γ2-adaptin, a putative member of the clathrin adaptor proteins responsible for protein sorting and trafficking, as a specific binding partner of L protein. Evidence for a physic…

Hepatitis B virusVesicle-associated membrane protein 8ImmunoprecipitationImmunologyGolgi ApparatusTransfectionmedicine.disease_causeMicrobiologyClathrinChromatography AffinityCytosolViral Envelope ProteinsMutant proteinYeastsVirologyProtein targetingmedicineAnimalsBinding siteAdaptor Protein Complex gamma SubunitsBinding SitesbiologyMembrane ProteinsPrecipitin TestsClathrinTransmembrane proteinVirus-Cell InteractionsCell biologyInsect ScienceCOS CellsMutationbiology.proteinClathrin adaptor proteinsProtein BindingJournal of Virology
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The viral chemokine MCK-2 of murine cytomegalovirus promotes infection as part of a gH/gL/MCK-2 complex.

2013

Human cytomegalovirus (HCMV) forms two gH/gL glycoprotein complexes, gH/gL/gO and gH/gL/pUL(128,130,131A), which determine the tropism, the entry pathways and the mode of spread of the virus. For murine cytomegalovirus (MCMV), which serves as a model for HCMV, a gH/gL/gO complex functionally homologous to the HCMV gH/gL/gO complex has been described. Knock-out of MCMV gO does impair, but not abolish, virus spread indicating that also MCMV might form an alternative gH/gL complex. Here, we show that the MCMV CC chemokine MCK-2 forms a complex with the glycoprotein gH, a complex which is incorporated into the virion. We could additionally show that mutants lacking both, gO and MCK-2 are not ab…

Human cytomegalovirusViral DiseasesMuromegalovirusChemokinevirusesMurine Cytomegalovirus ; viral chemokine MCK-2 ; gH/gL/MCK-2 complexMiceViral Envelope ProteinsBiology (General)Cells Culturedchemistry.chemical_classificationMice Inbred BALB Cvirus diseasesHerpesviridae InfectionsRecombinant ProteinsSpecific Pathogen-Free OrganismsInfectious DiseasesLiverChemokines CCMedicineFemaleResearch ArticleQH301-705.5ImmunologyBiologyMicrobiologyVirusCell LineViral ProteinsMuromegalovirusGlycoprotein complexVirologyGeneticsmedicineAnimalsBiologyMolecular BiologyTropismMacrophagesVirionVirus InternalizationRC581-607medicine.diseasebiology.organism_classificationVirologyImmunity InnatechemistryCell cultureMutationMacrophages Peritonealbiology.proteinParasitologyProtein MultimerizationImmunologic diseases. AllergyGlycoprotein
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Low Density Lipoprotein Receptor-related Protein (LRP) Interacts with Presenilin 1 and Is a Competitive Substrate of the Amyloid Precursor Protein (A…

2005

Presenilin 1 (PS1) is a critical component of the gamma-secretase complex, which is involved in the cleavage of several substrates including the amyloid precursor protein (APP) and the Notch receptor. Recently, the low density receptor-related protein (LRP) has been shown to be cleaved by a gamma-secretase-like activity. We postulated that LRP may interact with PS1 and tested its role as a competitive substrate for gamma-secretase. In this report we show that LRP colocalizes and interacts with endogenous PS1 using coimmunoprecipitation and fluorescence lifetime imaging microscopy. In addition, we found that gamma-secretase active site inhibitors do not disrupt the interaction between LRP an…

ImmunoprecipitationNotch signaling pathwayMice TransgenicBinding CompetitiveBiochemistryPresenilinCell LineSubstrate SpecificityRats Sprague-DawleyAmyloid beta-Protein PrecursorMiceEndopeptidasesmental disordersPresenilin-1Amyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansBinding siteMolecular BiologyBrain ChemistryBinding SitesbiologyChemistryMembrane ProteinsCell BiologyRatsnervous system diseasesCell biologyTransmembrane domainBiochemistryMultiprotein ComplexesLDL receptorbiology.proteinlipids (amino acids peptides and proteins)Amyloid Precursor Protein SecretasesAmyloid precursor protein secretaseLow Density Lipoprotein Receptor-Related Protein-1Journal of Biological Chemistry
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Revisited BIA-MS combination: Entire "on-a-chip" processing leading to the proteins identification at low femtomole to sub-femtomole levels

2008

International audience; We present the results of a study in which biomolecular interaction analysis (BIA, Biacore 2000) was combined with mass spectrometry (MS) using entire "on-a-chip" procedure. Most BIA-MS studies included an elution step of the analyte prior MS analysis. Here, we report a low-cost approach combining Biacore analysis with homemade chips and MS in situ identification onto the chips without elution step. First experiments have been made with rat serum albumin to determine the sensitivity and validation of the concept has been obtained with an antibody/antigen couple. Our "on-a-chip" procedure allowed complete analysis by MS-MS of the biochip leading to protein identificat…

In situMALDI-TOFAnalyte[ SDV.BBM.BP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsBiomedical EngineeringBiophysicsAnalytical chemistrySPRBiosensing TechniquesMass spectrometry01 natural sciencesSensitivity and Specificity03 medical and health sciencesProtein Interaction MappingElectrochemistryNanotechnologyBIA-MSBiochipChromatography High Pressure Liquid030304 developmental biology0303 health sciencesChromatographyprotein complexesElutionChemistryMicrochemistry010401 analytical chemistryMs analysisReproducibility of ResultsGeneral MedicineEquipment DesignMicrofluidic Analytical Techniques0104 chemical sciencesEquipment Failure Analysis[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMatrix-assisted laser desorption/ionizationSAMSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationBiotechnology
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Lipoprotein-induced phenoloxidase-activity in tarantula hemocyanin.

2015

Phenoloxidases play vital roles in invertebrate innate immune reactions, wound closure and sclerotization processes in arthropods. In chelicerates, where phenoloxidases are lacking, phenoloxidase-activity can be induced in the oxygen carrier hemocyanin in vitro by proteolytic cleavage, incubation with the artificial inducer SDS, or lipids. The role of protein-protein interaction has up to now received little attention. This is remarkable, as lipoproteins - complexes of proteins and lipids - are present at high concentrations in arthropod hemolymph. We characterized the three lipoproteins present in tarantula hemolymph, two high-density lipoproteins and one very high-density lipoprotein, and…

Innate immune systemChemistryMonophenol Monooxygenasemedicine.medical_treatmentLipoproteinsBiophysicsHemocyaninSpidersCleavage (embryo)BiochemistryMicelleIn vitroAnalytical ChemistryArthropod ProteinsBiochemistryMultiprotein ComplexesHemolymphHemocyaninsmedicineAnimalslipids (amino acids peptides and proteins)InducerMolecular BiologyLipoproteinBiochimica et biophysica acta
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