Search results for "STING protein"

showing 10 items of 68 documents

The Nonbilayer Lipid MGDG and the Major Light-Harvesting Complex (LHCII) Promote Membrane Stacking in Supported Lipid Bilayers.

2018

The thylakoid membrane of algae and land plants is characterized by its intricate architecture, comprising tightly appressed membrane stacks termed grana. The contributions of individual components to grana stack formation are not yet fully elucidated. As an in vitro model, we use supported lipid bilayers made of thylakoid lipid mixtures to study the effect of major light-harvesting complex (LHCII), different lipids, and ions on membrane stacking, seen as elevated structures forming on top of the planar membrane surface in the presence of LHCII protein. These structures were examined by confocal laser scanning microscopy, atomic force microscopy, and fluorescence recovery after photobleachi…

0106 biological sciences0301 basic medicineMicroscopy ConfocalChemistryLipid BilayersStackingLight-Harvesting Protein ComplexesPeasfood and beveragesFluorescence recovery after photobleachingMicroscopy Atomic Force01 natural sciencesBiochemistryLight-harvesting complexDiglycerides03 medical and health sciences030104 developmental biologyGlycolipidMembraneThylakoidConfocal laser scanning microscopyBiophysicslipids (amino acids peptides and proteins)Lipid bilayer010606 plant biology & botanyBiochemistry
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Functional rearrangement of the light-harvesting antenna upon state transitions in a green alga

2014

AbstractState transitions in the green alga Chlamydomonas reinhardtii serve to balance excitation energy transfer to photosystem I (PSI) and to photosystem II (PSII) and possibly play a role as a photoprotective mechanism. Thus, light-harvesting complex II (LHCII) can switch between the photosystems consequently transferring more excitation energy to PSII (state 1) or to PSI (state 2) or can end up in LHCII-only domains. In this study, low-temperature (77 K) steady-state and time-resolved fluorescence measured on intact cells of Chlamydomonas reinhardtii shows that independently of the state excitation energy transfer from LHCII to PSI or to PSII occurs on two main timescales of <15 ps and …

0106 biological sciencesPhotosystem IIEnergy transferBiophysicsLight-Harvesting Protein ComplexesphotosystemChlamydomonas reinhardtiiPhotosystem IPhotochemistry01 natural sciences03 medical and health sciencesstate transitionsgreen algaSDG 7 - Affordable and Clean Energy030304 developmental biologyPhotosystem0303 health sciencesenergy transfer/dk/atira/pure/sustainabledevelopmentgoals/affordable_and_clean_energybiologyPhotosystem I Protein ComplexChemistryta1182Photosystem II Protein ComplexState (functional analysis)biology.organism_classificationFluorescenceCell BiophysicsAtomic physicsExcitationChlamydomonas reinhardtii010606 plant biology & botanyBiophysical journal
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The Recent Development of a Sweet-Tasting Brazzein and its Potential Industrial Applications

2016

International audience; Brazzein is a small heat- and pH-stable sweet-tasting protein isolated from the West African plant, Pentadiplandra brazzeana. Brazzein combines a highly sweet potency, a long history of human consumption, and a remarkable stability, giving it great potential as a natural sweetener. Due to the difficulties of obtaining brazzein from its natural source, several efforts have been made to express brazzein using various heterologous expression systems. This chapter describes the biochemical, structural, sensory, and physiological properties of brazzein. We will summarize the current knowledge of the structure-activity relationship of brazzein. The biotechnological product…

0301 basic medicine0106 biological sciences[ SDV.AEN ] Life Sciences [q-bio]/Food and Nutritionreceiver01 natural sciences03 medical and health sciences0404 agricultural biotechnology010608 biotechnologygoût sucréBrazzeinSweet-tasting proteinHigh-potency sweetenersPentadiplandra030304 developmental biology2. Zero hunger0303 health sciencesbiologySweet-taste receptorStructure-function relationshipfood and beverages04 agricultural and veterinary sciencesbiology.organism_classification040401 food scienceWest african[SDV.AEN] Life Sciences [q-bio]/Food and Nutrition030104 developmental biologyprotéinehigh-potency sweetenerNatural sourcebiology.proteinBrazzeinBiochemical engineeringproteinédulcorant intenserécepteur[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
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The N-terminal domain of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for its acclimative proteolysis.

2000

AbstractVariations in the amount of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for regulation of the uptake of light into photosystem II. An endogenous proteolytic system was found to be involved in the degradation of LHCII in response to elevated light intensities and the proteolysis was shown to be under tight regulation [Yang, D.-H. et al. (1998) Plant Physiol. 118, 827–834]. In this study, the substrate specificity and recognition site towards the protease were examined using reconstituted wild-type and mutant recombinant LHCII. The results show that the LHCII apoprotein and the monomeric form of the holoprotein are targeted for proteolysis while t…

Acclimative proteaseChlorophyll aN-terminal domainPhotosystem IImedicine.medical_treatmentProteolysisMutantMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsBiophysicsLight-Harvesting Protein ComplexesRecognition siteEndogenyLight-harvesting complex IIBiochemistrylaw.inventionchemistry.chemical_compoundStructural BiologylawSpinacia oleraceaGeneticsmedicineAmino Acid SequenceMolecular BiologyProteasemedicine.diagnostic_testSequence Homology Amino AcidChemistryBinding proteinHydrolysisPhotosystem II Protein ComplexCell BiologyBiochemistryRecombinant light-harvesting complex IIProteolysisRecombinant DNAFEBS letters
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Folding in vitro of light-harvesting chlorophyll a/b protein is coupled with pigment binding.

2002

The major light-harvesting chlorophyll a/b protein (LHCIIb) of the plant photosynthetic apparatus is able to self-organise in vitro. When the recombinant apoprotein, Lhcb1, is solubilised in the denaturing detergent sodium (or lithium) dodecylsulfate (SDS or LDS) and then mixed with chlorophylls and carotenoids under renaturing conditions, structurally authentic LHCIIb forms. Assembly of functional LHCIIb, as indicated by the establishment of energy transfer between complex-bound chlorophyll molecules, occurs in two apparent kinetic steps with time constants of 10 to 30 seconds and 50 to 300 seconds, depending on the reaction conditions. Here, we use circular dichroism (CD) in the far-UV ra…

Chlorophyll aCircular dichroismProtein FoldingCircular DichroismPigment bindingProtein domainPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesPhotochemistryPhotosynthesisProtein Structure SecondaryRecombinant Proteinschemistry.chemical_compoundPigmentchemistryStructural BiologyChlorophyllvisual_artvisual_art.visual_art_mediumMolecular BiologyProtein secondary structureMicellesSequence DeletionJournal of molecular biology
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Synthesis and Functional Reconstitution of Light-Harvesting Complex II into Polymeric Membrane Architectures.

2015

One of most important processes in nature is the harvesting and dissipation of solar energy with the help of light-harvesting complex II (LHCII). This protein, along with its associated pigments, is the main solar-energy collector in higher plants. We aimed to generate stable, highly controllable, and sustainable polymer-based membrane systems containing LHCII-pigment complexes ready for light harvesting. LHCII was produced by cell-free protein synthesis based on wheat-germ extract, and the successful integration of LHCII and its pigments into different membrane architectures was monitored. The unidirectionality of LHCII insertion was investigated by protease digestion assays. Fluorescence …

Chlorophyll bChlorophyllChlorophyll aCell-Free SystemPolymersLipid BilayersLight-Harvesting Protein ComplexesGeneral ChemistryPhotochemistryFluorescenceCatalysisFluorescence spectroscopyFluorescenceLight-harvesting complexchemistry.chemical_compoundMembraneSpectrometry FluorescencechemistryChlorophyllBiophysicsLipid bilayerPeptide HydrolasesAngewandte Chemie (International ed. in English)
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Light-harvesting chlorophyll a/b-binding protein stably inserts into etioplast membranes supplemented with Zn-pheophytin a/b.

1997

Light-harvesting chlorophyll a/b-binding protein, LHCP, or its precursor, pLHCP, cannot be stably inserted into barley etioplast membranes in vitro. However, when these etioplast membranes are supplemented with the chlorophyll analogs Zn-pheophytin a/b, synthesized in situ from Zn-pheophorbide a/b and digeranyl pyrophosphate, pLHCP is inserted into a protease-resistant state. This proves that chlorophyll is the only component lacking in etioplast membranes that is necessary for stable LHCP insertion. Synthesis of Zn-pheophytin b alone promotes insertion of LHCP in vitro into a protease-resistant state, whereas synthesis of Zn-pheophytin a alone does not. Insertion of pLHCP into etioplast me…

Chlorophyll bChlorophyllChlorophyll aChlorophyll APhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesPheophytinsCell BiologyBiologyPlantsBiochemistrychemistry.chemical_compoundB vitaminsZincMembraneGreeningBiochemistrychemistryEtioplastChlorophyllThylakoidMolecular BiologyThe Journal of biological chemistry
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Determination of relative chlorophyll binding affinities in the major light-harvesting chlorophyll a/b complex.

2002

The major light-harvesting complex (LHCIIb) of photosystem II can be reconstituted in vitro from its recombinant apoprotein in the presence of a mixture of carotenoids and chlorophylls a and b. By varying the chlorophyll a/b ratio in the reconstitution mixture, the relative amounts of chlorophyll a and chlorophyll b bound to LHCIIb can be changed. We have analyzed the chlorophyll stoichiometry in recombinant wild type and mutant LHCIIb reconstituted at different chlorophyll a/b ratios in order to assess relative affinities of the chlorophyll-binding sites. This approach reveals five sites that exclusively bind chlorophyll b. Another site exhibits a slight preference of chlorophyll b over ch…

Chlorophyll bChlorophyllChlorophyll aPhotosystem IIPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiologyBiochemistrychemistry.chemical_compoundChlorophyll bindingBinding siteMolecular BiologyCarotenoidchemistry.chemical_classificationBinding SitesPeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsB vitaminsKineticsBiochemistrychemistryAmino Acid SubstitutionChlorophyllMutagenesis Site-DirectedThe Journal of biological chemistry
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Consecutive binding of chlorophylls a and b during the assembly in vitro of light-harvesting chlorophyll-a/b protein (LHCIIb).

2006

The apoprotein of the major light-harvesting chlorophyll a/b complex (LHCIIb) is post-translationally imported into the chloroplast, where membrane insertion, protein folding, and pigment binding take place. The sequence and molecular mechanism of the latter steps is largely unknown. The complex spontaneously self-organises in vitro to form structurally authentic LHCIIb upon reconstituting the unfolded recombinant protein with the pigments chlorophyll a, b, and carotenoids in detergent micelles. Former measurements of LHCIIb assembly had revealed two apparent kinetic phases, a faster one (tau1) in the range of 10 s to 1 min, and a slower one (tau2) in the range of several min. To unravel th…

Chlorophyll bChlorophyllChlorophyll aTime FactorsPigment bindingLight-Harvesting Protein ComplexesModels BiologicalFluorescencechemistry.chemical_compoundStructural BiologyChlorophyll bindingAnimalsProtein Structure QuaternaryMolecular BiologyChlorophyll ACircular DichroismLight-harvesting complexes of green plantsChloroplastB vitaminsKineticsBiochemistrychemistryEnergy TransferChlorophyllBiophysicsChlamydomonas reinhardtiiProtein BindingJournal of molecular biology
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Refinement of a structural model of a pigment-protein complex by accurate optical line shape theory and experiments.

2007

Time-local and time-nonlocal theories are used in combination with optical spectroscopy to characterize the water-soluble chlorophyll binding protein complex (WSCP) from cauliflower. The recombinant cauliflower WSCP complexes reconstituted with either chlorophyll b (Chl b) or Chl a/Chl b mixtures are characterized by absorption spectroscopy at 77 and 298 K and circular dichroism at 298 K. On the basis of the analysis of these spectra and spectra reported for recombinant WSCP reconstituted with Chl a only (Hughes, J. L.; Razeghifard, R.; Logue, M.; Oakley, A.; Wydrzynski, T.; Krausz, E. J. Am. Chem. Soc. U.S.A. 2006, 128, 3649), the "open-sandwich" model proposed for the structure of the pig…

Chlorophyll bChlorophyllModels MolecularCircular dichroismOptics and PhotonicsAbsorption spectroscopyChemistryDimerExcitonChlorophyll ACircular DichroismSpectrum AnalysisStatic ElectricityLight-Harvesting Protein ComplexesBrassicaSpectral lineSurfaces Coatings and Filmschemistry.chemical_compoundCrystallographyKineticsModels ChemicalMaterials ChemistryChlorophyll bindingPhysical and Theoretical ChemistrySpectroscopyThe journal of physical chemistry. B
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