Search results for "chloroplast"

showing 10 items of 145 documents

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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Exchange of Pigment-Binding Amino Acids in Light-Harvesting Chlorophyll a/b Protein

1999

Four amino acids in the major light-harvesting chlorophyll (Chl) a/b complex (LHCII) that are thought to coordinate Chl molecules have been exchanged with amino acids that presumably cannot bind Chl. Amino acids H68, Q131, Q197, and H212 are positioned in helixes B, C, A, and D, respectively, and, according to the LHCII crystal structure [Kühlbrandt, W., et al. (1994) Nature 367, 614-621], coordinate the Chl molecules named a(5), b(6), a(3), and b(3). Moreover, a double mutant was analyzed carrying exchanges at positions E65 and H68, presumably affecting Chls a(4) and a(5). All mutant proteins could be reconstituted in vitro with pigments, although the thermal stability of the resulting mut…

ChlorophyllChloroplastsMacromolecular SubstancesStereochemistryMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsPigment bindingLight-Harvesting Protein ComplexesTrimerBiochemistrychemistry.chemical_compoundAmino Acid SequenceAmino AcidsPeptide sequencePlant Proteinschemistry.chemical_classificationBinding SitesChlorophyll APeasPhotosystem II Protein Complexfood and beveragesAmino acidChloroplastB vitaminsAmino Acid SubstitutionchemistryChlorophyllThylakoidMutagenesis Site-DirectedCarrier ProteinsBiochemistry
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Inactivation of a plastid evolutionary conserved gene affects PSII electron transport, life span and fitness of tobacco plants

2007

Chloroplasts contain a plastoquinone-NADH-oxidoreductase (Ndh) complex involved in protection against stress and the maintenance of cyclic electron flow. Inactivation of the Ndh complex delays the development of leaf senescence symptoms. Chlorophyll a fluorescence measurements, blue native gel electrophoresis, immunodetection and other techniques were employed to study tobacco (Nicotiana tabacum) Ndh-defective mutants (DeltandhF). The DeltandhF mutants compared with wild-type plants presented: (i) higher photosystem II : photosystem I (PSII : PSI) ratios; (ii) similar or higher levels of ascorbate, carotenoids, thylakoid peroxidase and superoxide dismutase, yield (Phi(PSII)) and maximal pho…

ChlorophyllChloroplastsTime FactorsLightPhotosystem IIPhysiologyNicotiana tabacumPlant SciencePhotosystem IPhotosynthesisAntioxidantsFluorescenceElectron Transportchemistry.chemical_compoundTobaccoBotanyGene SilencingPhotosynthesisChlorophyll fluorescencePlant ProteinsPhotosystem I Protein ComplexbiologyChlorophyll AReproductionPhotosystem II Protein Complexfood and beveragesNADH Dehydrogenasebiology.organism_classificationChloroplastPhenotypechemistryChlorophyllThylakoidBiophysicsNew Phytologist
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Calcium signatures and signaling in cytosol and organelles of tobacco cells induced by plant defense elicitors

2011

Calcium signatures induced by two elicitors of plant defense reactions, namely cryptogein and oligogalacturonides, were monitored at the subcellular level, using apoaequorin-transformed Nicotiana tabacum var Xanthi cells, in which the apoaequorin calcium sensor was targeted either to cytosol, mitochondria or chloroplasts. Our study showed that both elicitors induced specific Ca2+ signatures in each compartment, with the most striking difference relying on duration. Common properties also emerged from the analysis of Ca2+ signatures: both elicitors induced a biphasic cytosolic [Ca2+] elevation together with a single mitochondrial [Ca2+] elevation concomitant with the first cytosolic [Ca2+] p…

ChlorophyllChloroplastsTime FactorsPhysiology[SDV]Life Sciences [q-bio]Nicotiana tabacumAequorinMitochondrionMITOCHONDRIALAntiportersCA2+CytosolPlant defenseINTACT CHLOROPLASTSCation Transport ProteinsCalcium signalingRECOMBINANT AEQUORINDEATHfood and beveragesARABIDOPSISOligogalacturonidesMitochondriaChloroplastBiochemistry[SDE]Environmental SciencesCryptogeinPhytophthorachemistry.chemical_elementCalciumBiologyChloroplastFluorescenceFungal ProteinsPHOTOSYSTEM-IIPlant CellsTobaccoOrganelle[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyCalcium SignalingMolecular BiologyHYPERSENSITIVE RESPONSENITRIC-OXIDECell MembraneCell Biologybiology.organism_classificationSALICYLIC-ACIDOxygenCytosolchemistryBiophysicsbiology.proteinCalciumCell Calcium
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De-epoxidation of Violaxanthin in Light-harvesting Complex I Proteins

2004

The conversion of violaxanthin (Vx) to zeaxanthin (Zx) in the de-epoxidation reaction of the xanthophyll cycle plays an important role in the protection of chloroplasts against photooxidative damage. Vx is bound to the antenna proteins of both photosystems. In photosystem II, the formation of Zx is essential for the pH-dependent dissipation of excess light energy as heat. The function of Zx in photosystem I is still unclear. In this work we investigated the de-epoxidation characteristics of light-harvesting complex proteins of photosystem I (LHCI) under in vivo and in vitro conditions. Recombinant LHCI (Lhcal-4) proteins were reconstituted with Vx and lutein, and the convertibility of Vx wa…

ChlorophyllLuteinPhotosystem IIPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesXanthophyllsPhotosystem IThylakoidsBiochemistrychemistry.chemical_compoundSolanum lycopersicumSpinacia oleraceaEscherichia coliMolecular BiologyPhotosystemchemistry.chemical_classificationBinding SitesPhotosystem I Protein ComplexChemistryfood and beveragesPigments BiologicalCell Biologybeta CaroteneRecombinant ProteinsChloroplastKineticsBiochemistryXanthophyllThylakoidEpoxy CompoundsApoproteinsViolaxanthinJournal of Biological Chemistry
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Early folding events during light harvesting complex II assembly in vitro monitored by pulsed electron paramagnetic resonance

2016

Efficient energy transfer in the major light harvesting complex II (LHCII) of green plants is facilitated by the precise alignment of pigments due to the protein matrix they are bound to. Much is known about the import of the LHCII apoprotein into the chloroplast via the TOC/TIC system and its targeting to the thylakoid membrane but information is sparse about when and where the pigments are bound and how this is coordinated with protein folding. In vitro, the LHCII apoprotein spontaneously folds and binds its pigments if the detergent-solubilized protein is combined with a mixture of chlorophylls a and b and carotenoids. In the present work, we employed this approach to study apoprotein fo…

ChlorophyllModels Molecular0301 basic medicineProtein FoldingPigment bindingLight-Harvesting Protein ComplexesBiophysicsBiochemistrylaw.invention03 medical and health scienceslawElectron paramagnetic resonancePlant ProteinsPulsed EPRChemistryElectron Spin Resonance SpectroscopyPeasPhotosystem II Protein ComplexCell BiologyProtein tertiary structureProtein Structure TertiaryChloroplastFolding (chemistry)KineticsCrystallography030104 developmental biologyEnergy TransferThylakoidProtein foldingApoproteinsProtein BindingBiochimica et Biophysica Acta (BBA) - Bioenergetics
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Modulation of the growth and metabolic response of cyanobacteria by the multifaceted activity of naringenin

2017

The interactions between the plant-derived bioflavonoid, naringenin, and prokaryotic microalgae representatives (cyanobacteria), were investigated with respect to its influence on the growth and metabolic response of these microorganisms. To achieve reliable results, the growth of cyanobacteria was determined based on measurements of chlorophyll content, morphological changes were assessed through microscopic observations, and the chemical response of cells was determined using liquid and gas chromatography (HPLC; GC-FID). The results show that micromolar levels of naringenin stimulated the growth of cyanobacteria. Increased growth was observed for halophilic strains at naringenin concentra…

ChlorophyllPigments0301 basic medicineCyanobacteriaNaringeninExopolysaccharidesChloroplastsMicroorganismCellGlycobiologyMarine and Aquatic Scienceslcsh:MedicineFresh WaterPlant ScienceBiochemistrychemistry.chemical_compoundElectron MicroscopyNostoclcsh:ScienceLiquid ChromatographyMicroscopyMultidisciplinarybiologyChemistryChromatographic Techniquesfood and beveragesHalophilemedicine.anatomical_structureBiochemistryFlavanonesPhysical SciencesScanning Electron MicroscopyCellular Structures and OrganellesCellular TypesResearch ArticleFreshwater EnvironmentsChromatography GasPlant Cell BiologyMaterials Science030106 microbiologyCyanobacteriaResearch and Analysis MethodsCell wallExcretion03 medical and health sciencesPolysaccharidesPlant CellsmedicineMaterials by AttributeBacteriaOrganic PigmentsEcology and Environmental Scienceslcsh:ROrganismsBiology and Life SciencesAquatic EnvironmentsCell Biologybiology.organism_classificationAnabaenaHigh Performance Liquid Chromatography030104 developmental biologyEarth Scienceslcsh:QBacteriaChromatography LiquidNostoc muscorumPLOS ONE
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Chlamydomonas reinhardtii in the landscape of pigments.

2004

▪ Abstract  This review focuses on the biosynthesis of pigments in the unicellular alga Chlamydomonas reinhardtii and their physiological and regulatory functions in the context of information gathered from studies of other photosynthetic organisms. C. reinhardtii is serving as an important model organism for studies of photosynthesis and the pigments associated with the photosynthetic apparatus. Despite extensive information pertaining to the biosynthetic pathways critical for making chlorophylls and carotenoids, we are just beginning to understand the control of these pathways, the coordination between pigment and apoprotein synthesis, and the interactions between the activities of these…

ChlorophyllRhodopsinNuclear geneChloroplastsved/biology.organism_classification_rank.speciesLight-Harvesting Protein ComplexesProtozoan ProteinsChlamydomonas reinhardtiiPhotosynthesisModels Biologicalchemistry.chemical_compoundHemiterpenesLycopeneBiosynthesisIsomerismPentanesBotanyGeneticsButadienesAnimalsPhotosynthesisModel organismCarotenoidPlant Proteinschemistry.chemical_classificationCell Nucleusbiologyved/biologyPigments Biologicalbiology.organism_classificationCarotenoidsChloroplastOxygenCytochrome b6f ComplexchemistryBiochemistryXanthophyllPhotoreceptor Cells InvertebrateChlamydomonas reinhardtiiAnnual review of genetics
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The intensification of absorbance changes in leaves by light-dispersion

1979

In dispersive samples, like leaves, the absorbance of pigments is intensified. The intensification is due to a longer optical path through the dispersive sample. However, in chloroplast suspensions the optical path is not much longer than in clear solutions. The factor of intensification β (=the lengthening of the optical path) is calculated by comparing the absorbance of leaves and the absorbance of chloroplast suspensions with equal pigment-content. This method also includes the influence of possible sieve effects which could decrease absorbance. The measurements are carried out with high- and low-light leaves of different thickness and pigment content. The intensification of absorbance w…

ChloroplastAbsorbanceCytochrome fPigmentChromatographyChemistryvisual_artLight dispersionGeneticsAnalytical chemistryvisual_art.visual_art_mediumsense organsPlant SciencePlanta
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The molecular architecture of the thylakoid membrane from various classes of eukaryotic algae

1990

There is convincing consensus that the photosynthetic apparatus is of prokaryotic origin. The wide variety of algal plastids is mostly assumed to be the result of different endocytological events. Chloroplasts surrounded by two membranes as in rhodophytes and chlorophytes were considered as the association of a prokaryotic symbiont and a eukaryotic host, whereas algae having a chloroplast surrounded with more than two membranes can be delineated from an endocytological event of two eukaryotes (see S. Gibbs in this volume). Since chlorophyll b was neither combined with chlorophyll c nor with phycobiliproteins it was proposed that all present day chloroplasts can be integrated in three lines.…

ChloroplastChlorophyll bchemistry.chemical_compoundAlgaebiologychemistryPhycobiliproteinThylakoidBotanyChlorophyll cPlastidPhotosynthesisbiology.organism_classification
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