Search results for "STING protein"

showing 10 items of 68 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

How Fragile We Are: Influence of Stimulator of Interferon Genes (STING) Variants on Pathogen Recognition and Immune Response Efficiency.

2022

AbstractThe STimulator of INterferon Genes (STING) protein is a cornerstone of the human immune response. Its activation by cGAMP upon the presence of cytosolic DNA stimulates the production of type I interferons and inflammatory cytokines which are crucial for protecting cells from infections. STING signaling pathway can also influence both tumor-suppressive and tumor-promoting mechanisms, rendering it an appealing target for drug design. In the human population, several STING variants exist and exhibit dramatic differences in their activity, impacting the efficiency of the host defense against infections. Understanding the differential molecular mechanisms exhibited by these variants is o…

General Chemical EngineeringPopulationLibrary and Information SciencesBiologyProinflammatory cytokinemutation.Immune system[CHIM]Chemical SciencesHumanseducationPathogenwild-typeeducation.field_of_studyWild typeMembrane ProteinsGeneral ChemistrySTING proteinImmunity InnateComputer Science ApplicationsStingmolecular dynamics simulationSettore CHIM/03 - Chimica Generale E InorganicaStimulator of interferon genesImmunologyInterferonsSignal transductionJournal of chemical information and modeling
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

Bio serves nano: biological light-harvesting complex as energy donor for semiconductor quantum dots.

2012

Light-harvesting complex (LHCII) of the photosynthetic apparatus in plants is attached to type-II core-shell CdTe/CdSe/ZnS nanocrystals (quantum dots, QD) exhibiting an absorption band at 710 nm and carrying a dihydrolipoic acid coating for water solubility. LHCII stays functional upon binding to the QD surface and enhances the light utilization of the QDs significantly, similar to its light-harvesting function in photosynthesis. Electronic excitation energy transfer of about 50% efficiency is shown by donor (LHCII) fluorescence quenching as well as sensitized acceptor (QD) emission and corroborated by time-resolved fluorescence measurements. The energy transfer efficiency is commensurable …

Light-Harvesting Protein ComplexesSulfidesPhotochemistryAbsorptionLight-harvesting complexQuantum DotsElectrochemistryCadmium CompoundsGeneral Materials ScienceAbsorption (electromagnetic radiation)Selenium CompoundsSpectroscopyFluorescent Dyesbusiness.industryChemistryPeasSurfaces and InterfacesCondensed Matter PhysicsFluorescenceAcceptorNanocrystalEnergy TransferSemiconductorsAbsorption bandQuantum dotZinc CompoundsOptoelectronicsTelluriumbusinessVisible spectrumLangmuir : the ACS journal of surfaces and colloids
researchProduct

Energy Transfer between Surface-Immobilized Light-Harvesting Chlorophyll a/b Complex (LHCII) Studied by Surface Plasmon Field-Enhanced Fluorescence S…

2010

The major light-harvesting chlorophyll a/b complex (LHCII) of the photosynthetic apparatus in green plants can be viewed as a protein scaffold binding and positioning a large number of pigment molecules that combines rapid and efficient excitation energy transfer with effective protection of its pigments from photobleaching. These properties make LHCII potentially interesting as a light harvester (or a model thereof) in photoelectronic applications. Most of such applications would require the LHCII to be immobilized on a solid surface. In a previous study we showed the immobilization of recombinant LHCII on functionalized gold surfaces via a 6-histidine tag (His tag) in the protein moiety. …

Models MolecularChlorophyll aProtein ConformationSurface PropertiesLight-Harvesting Protein ComplexesPhotochemistryFluorescence spectroscopyAbsorptionchemistry.chemical_compoundFluorescence Resonance Energy TransferElectrochemistryMoleculeGeneral Materials ScienceSpectroscopyFluorescent DyesSurface plasmonPeasSurfaces and InterfacesEnzymes ImmobilizedCondensed Matter PhysicsPhotobleachingFluorescenceAcceptorKineticsB vitaminschemistryLangmuir
researchProduct

Thermally Activated Superradiance and Intersystem Crossing in the Water-Soluble Chlorophyll Binding Protein

2009

The crystal structure of the class IIb water-soluble chlorophyll binding protein (WSCP) from Lepidium virginicum is used to model linear absorption and circular dichroism spectra as well as excited state decay times of class IIa WSCP from cauliflower reconstituted with chlorophyll (Chl) a and Chl b. The close agreement between theory and experiment suggests that both types of WSCP share a common Chl binding motif, where the opening angle between pigment planes in class IIa WSCP should not differ by more than 10 degrees from that in class IIb. The experimentally observed (Schmitt et al. J. Phys. Chem. B 2008, 112, 13951) decrease in excited state lifetime of Chl a homodimers with increasing …

Models MolecularCircular DichroismDimerExcitonStatic ElectricityLight-Harvesting Protein ComplexesTemperatureWaterCrystal structureCrystallography X-RayPhotochemistryLepidiumSurfaces Coatings and Filmschemistry.chemical_compoundCrystallographyIntersystem crossingSolubilitychemistryChlorophyllExcited stateMaterials ChemistryChlorophyll bindingQuantum TheoryPhysical and Theoretical ChemistryAbsorption (chemistry)The Journal of Physical Chemistry B
researchProduct

Lhca5 interaction with plant photosystem I

2006

AbstractIn the outer antenna (LHCI) of higher plant photosystem I (PSI) four abundantly expressed light-harvesting protein of photosystem I (Lhca)-type proteins are organized in two heterodimeric domains (Lhca1/Lhca4 and Lhca2/Lhca3). Our cross-linking studies on PSI-LHCI preparations from wildtype Arabidopsis and pea plants indicate an exclusive interaction of the rarely expressed Lhca5 light-harvesting protein with LHCI in the Lhca2/Lhca3-site. In PSI particles with an altered LHCI composition Lhca5 assembles in the Lhca1/Lhca4 site, partly as a homodimer. This flexibility indicates a binding-competitive model for the LHCI assembly in plants regulated by molecular interactions of the Lhca…

Models MolecularPhotosystem IArabidopsisLight-Harvesting Protein ComplexesBiophysicsPhotosystem IBiochemistrychemistry.chemical_compoundLight harvesting complex IStructural BiologyArabidopsisGeneticsMolecular BiologyLhca5Molecular interactionsPhotosystem I Protein ComplexbiologyArabidopsis ProteinsPeasWild typefood and beveragesArabidopsis ProteinsCell BiologyLight-Harvesting Protein Complexesbiology.organism_classificationCrystallographychemistryChlorophyllBiophysicsLight-harvesting complex ICross-linkingFEBS Letters
researchProduct

The non-bilayer lipid MGDG stabilizes the major light-harvesting complex (LHCII) against unfolding.

2017

Abstract In the photosynthetic apparatus of plants a high proportion of LHCII protein is needed to integrate 50% non-bilayer lipid MGDG into the lamellar thylakoid membrane, but whether and how the stability of the protein is also affected is not known. Here we use single-molecule force spectroscopy to map the stability of LHCII against mechanical unfolding along the polypeptide chain as a function of oligomerization state and lipid composition. Comparing unfolding forces between monomeric and trimeric LHCII demonstrates that the stability does not increase significantly upon trimerization but can mainly be correlated with specific contact sites between adjacent monomers. In contrast, unfol…

Models MolecularProtein ConformationScienceGalactolipidsQRLight-Harvesting Protein ComplexesPeasThylakoidsArticle580 Pflanzen (Botanik)Medicinelipids (amino acids peptides and proteins)580 Botanical sciencesPlant ProteinsProtein UnfoldingScientific reports
researchProduct