Search results for "protein complexes"

showing 10 items of 113 documents

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
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct

Human Hsp60 with Its Mitochondrial Import Signal Occurs in Solution as Heptamers and Tetradecamers Remarkably Stable over a Wide Range of Concentrati…

2014

It has been established that Hsp60 can accumulate in the cytosol in various pathological conditions, including cancer and chronic inflammatory diseases. Part or all of the cytosolic Hsp60 could be naive, namely, bear the mitochondrial import signal (MIS), but neither the structure nor the in solution oligomeric organization of this cytosolic molecule has still been elucidated. Here we present a detailed study of the structure and self-organization of naive cytosolic Hsp60 in solution. Results were obtained by different biophysical methods (light and X ray scattering, single molecule spectroscopy and hydrodynamics) that all together allowed us to assay a wide range of concentrations of Hsp60…

LightCancer Treatmentlcsh:MedicinePlasma protein bindingMitochondrionBiochemistrySmall-Angle ScatteringCell-free systemScatteringchemistry.chemical_compoundCytosolProtein structureBasic Cancer ResearchMacromolecular Structure AnalysisMedicine and Health SciencesScattering RadiationHsp60 Gro EL Recombinant proteinslcsh:ScienceAdenosine TriphosphatasesMultidisciplinaryAqueous solutionMolecular StructurePhysicsElectromagnetic RadiationHydrolysisRecombinant ProteinsMitochondriaChemistryMonomerOncologyBiochemistryPhysical SciencesInterdisciplinary PhysicsHSP60Research ArticleProtein BindingProtein Structureanimal structuresBiophysicschemical and pharmacologic phenomenaBiologycomplex mixturesMitochondrial ProteinsHumansProtein InteractionsMolecular BiologyInflammationChemical PhysicsCell-Free Systemlcsh:RfungiLight ScatteringBiology and Life SciencesProteinsProtein ComplexesChaperonin 60Chaperone ProteinsCytosolSpectrometry FluorescencechemistryMolecular Complexeslcsh:QPLoS ONE
researchProduct

Insertion of light-harvesting chlorophyll a/b protein into the thylakoid

2000

The major light-harvesting chlorophyll a/b-binding protein (Lhcb1,2) of photosystem II is inserted into the thylakoid via the signal recognition particle dependent pathway. However, the mechanism by which the protein enters the membrane is at this time unknown. In order to define some topographical restrictions for this process, we constructed several recombinant derivatives of Lhcb1 carrying hexahistidine tags at either protein terminus or in the stromal loop domain. Additionally, green fluorescent protein (GFP) was fused to either terminus. None of the modifications significantly impair the pigment-binding properties of the protein in the in vitro reconstitution of LHCII. With the excepti…

LightPhotosystem IIRecombinant Fusion ProteinsGreen Fluorescent ProteinsPhotosynthetic Reaction Center Complex ProteinsMutantLight-Harvesting Protein ComplexesBiologyThylakoidsBiochemistryInsert (molecular biology)Green fluorescent proteinLight-harvesting complexchemistry.chemical_compoundNickelHistidinePlant ProteinsSignal recognition particlePeasPhotosystem II Protein ComplexBiological TransportIntracellular MembranesPigments BiologicalMolecular WeightLuminescent ProteinschemistryBiochemistryChlorophyllThylakoidMutationBiophysicsCarrier ProteinsEuropean Journal of Biochemistry
researchProduct

Predictive First-Principles Modeling of a Photosynthetic Antenna Protein: The Fenna–Matthews–Olson Complex

2020

High efficiency of light harvesting in photosynthetic pigment–protein complexes is governed by evolutionary-perfected protein-assisted tuning of individual pigment properties and interpigment interactions. Due to the large number of spectrally overlapping pigments in a typical photosynthetic complex, experimental methods often fail to unambiguously identify individual chromophore properties. Here, we report a first-principles-based modeling protocol capable of predicting properties of pigments in protein environment to a high precision. The technique was applied to successfully uncover electronic properties of the Fenna–Matthews–Olson (FMO) pigment–protein complex. Each of the three subunit…

Light-Harvesting Protein Complexes02 engineering and technologyMolecular Dynamics Simulation010402 general chemistryPhotosynthesis01 natural sciencesChlorobiProtein environmentBacterial ProteinsGeneral Materials SciencePhotosynthesisPhysical and Theoretical ChemistryBacteriochlorophyll AFenna-Matthews-Olson complexElectronic propertiesStrongly coupledChemistryCircular DichroismBacteriochlorophyll AChromophore021001 nanoscience & nanotechnology0104 chemical sciencesEnergy TransferChemical physicsQuantum TheoryGasessense organsExperimental methods0210 nano-technologyThe Journal of Physical Chemistry Letters
researchProduct