Search results for "Protein Complex"

showing 10 items of 154 documents

The Light-Harvesting Chlorophyll a/b Complex Can Be Reconstituted in Vitro from Its Completely Unfolded Apoprotein

2003

The major light-harvesting chlorophyll a/b protein (LHCIIb) of higher plants is one of the few membrane proteins that can be refolded in vitro. During folding, the apoprotein is assembled with pigments to form a structurally authentic and functional pigment--protein complex. All reconstitution procedures used so far include solubilization of the apoprotein in sodium dodecyl sulfate (SDS) where the protein adopts approximately half of its alpha-helical folding present in the native structure. This paper shows that this preformed alpha-helix is not a prerequisite for LHCIIb folding in vitro. The apoprotein can also be reconstituted starting from a solution in guanidinium hydrochloride (Gnd) w…

ChlorophyllProtein FoldingChlorophyll ACircular DichroismPhotosynthetic Reaction Center Complex ProteinsKineticsLight-Harvesting Protein Complexesfood and beveragesBiochemistryFluorescenceIn vitroFolding (chemistry)B vitaminschemistry.chemical_compoundPigmentSpectrometry FluorescenceBiochemistrychemistryMembrane proteinvisual_artvisual_art.visual_art_mediumSodium dodecyl sulfateApoproteinsBiochemistry
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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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p53-Mediated downregulation of H ferritin promoter transcriptional efficiency via NF-Y.

2008

The tumor suppressor protein p53 triggers many of the cellular responses to DNA damage by regulating the transcription of a series of downstream target genes. p53 acts on the promoter of the target genes by interacting with the trimeric transcription factor NF-Y. H ferritin promoter activity is tightly dependent on a multiprotein complex called Bbf; on this complex NF-Y plays a major role. The aim of this work was to study the modulation of H ferritin expression levels by p53. CAT reporter assays indicate that: (i) p53 overexpression strongly downregulates the transcriptional efficiency driven by an H ferritin promoter construct containing only the NF-Y recognition sequence and that the phe…

Chromatin ImmunoprecipitationMultiprotein complexTranscription GeneticDown-RegulationBiologyBiochemistryTranscriptional regulationDownregulation and upregulationTranscription (biology)Transcriptional regulationFerritin geneHumansElectrophoretic mobility shift assayp300-CBP Transcription FactorsPromoter Regions GeneticTranscription factorGeneFerritin gene; Transcriptional regulation; Transcriptional factorCell BiologyHCT116 CellsMolecular biologyGene Expression Regulation NeoplasticCCAAT-Binding FactorDoxorubicinTranscriptional factorApoferritinsTumor Suppressor Protein p53Chromatin immunoprecipitationHeLa CellsProtein Binding
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The inner nuclear membrane protein Src1 associates with subtelomeric genes and alters their regulated gene expression

2008

Inner nuclear membrane proteins containing a LEM (LAP2, emerin, and MAN1) domain participate in different processes, including chromatin organization, gene expression, and nuclear envelope biogenesis. In this study, we identify a robust genetic interaction between transcription export (TREX) factors and yeast Src1, an integral inner nuclear membrane protein that is homologous to vertebrate LEM2. DNA macroarray analysis revealed that the expression of the phosphate-regulated genes PHO11, PHO12, and PHO84 is up-regulated in src1Δ cells. Notably, these PHO genes are located in subtelomeric regions of chromatin and exhibit a perinuclear location in vivo. Src1 spans the nuclear membrane twice an…

Chromatin ImmunoprecipitationSaccharomyces cerevisiae ProteinsGenes FungalSaccharomyces cerevisiaeProtein Sorting SignalsBiologyArticleGenètica molecularProton-Phosphate SymportersGene Expression Regulation FungalGene expressionmedicineExpressió genèticaInner membraneNuclear proteinNuclear poreNuclear membraneResearch ArticlesNucleoplasmMembrane ProteinsNuclear ProteinsCell BiologyTelomereMolecular biologyChromatinProtein Structure TertiaryChromatinAlternative SplicingGenòmicamedicine.anatomical_structureMultiprotein ComplexesNuclear lamina
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Silica Entrapment for Significantly Stabilized, Energy-Conducting Light-Harvesting Complex (LHCII)

2014

The major light-harvesting chlorophyll a/b complex (LHCII) of the photosynthetic apparatus in green plants consists of a membrane protein and numerous noncovalently bound pigments that make up about one-third of the molecular mass of the pigment-protein complex. Due to this high pigment density, LHCII is potentially interesting as a light-harvesting component in synthetic constructs. However, for such applications its stability needs to be significantly improved. In this work, LHCII was dramatically stabilized by enclosing it within polymerizing colloidal silica. The entrapped LHCII stayed functional at 50 °C for up to 24 h instead of a few minutes in detergent solution and clearly showed e…

ChromatographyMolecular massChemistryColloidal silicaLight-Harvesting Protein ComplexesPhotosystem II Protein ComplexSurfaces and InterfacesSilicon DioxideCondensed Matter PhysicsPhotosynthesisLight-harvesting complexB vitaminsPigmentPolymerizationYield (chemistry)visual_artElectrochemistryBiophysicsvisual_art.visual_art_mediumGeneral Materials ScienceSpectroscopyLangmuir
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Thermal stability of trimeric light-harvesting chlorophyll a/b complex (LHCIIb) in liposomes of thylakoid lipids.

2006

The major light-harvesting chlorophyll a/b complex (LHCIIb) of photosystem (PS) II functions by harvesting light energy and by limiting and balancing the energy flow directed towards the PSI and PSII reaction centers. The complex is predominantly trimeric; however, the monomeric form may play a role in one or several of the regulatory functions of LHCIIb. In this work the dissociation temperature was measured of trimeric LHCIIb isolated from Pisum thylakoids and inserted into liposomes made of various combinations of thylakoid lipids at various protein densities. Dissociation was measured by monitoring a trimer-specific circular dichroism signal in the visible range. The LHCIIb density in t…

Circular dichroismBiophysicsLight-Harvesting Protein ComplexesTrimerPhotochemistryBiochemistryThylakoidsDissociation (chemistry)Membrane LipidsProtein Structure QuaternaryTrimerDiacylglycerol kinasePhotosystemPlant ProteinsLiposomeChemistryCircular DichroismLight harvesting complexes of photosystem II (LHCIIb)Peasfood and beveragesThermal stabilityCell BiologyLiposomeThylakoid lipidsB vitaminsThylakoidMultiprotein ComplexesLiposomesThermodynamicslipids (amino acids peptides and proteins)Biochimica et biophysica acta
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Tight DNA-protein complexes isolated from barley seedlings are rich in potential guanine quadruplex sequences

2020

Background The concept of chromatin domains attached to the nuclear matrix is being revisited, with nucleus described as a set of topologically associating domains. The significance of the tightly bound to DNA proteins (TBP), a protein group that remains attached to DNA after its deproteinization should be also revisited, as the existence of these interactions is in good agreement with the concept of the topologically associating domain. The work aimed to characterize the DNA component of TBP isolated from barley seedlings. Methods The tight DNA-protein complexes from the first leaves, coleoptiles, and roots of barley seedlings were isolated by purification with chromatography on nitrocell…

Circular dichroismGuaninelcsh:MedicinePlant ScienceGC-rich DNAG-quadruplexDeproteinisation-resistant DNA-protein complexesGeneral Biochemistry Genetics and Molecular Biology03 medical and health scienceschemistry.chemical_compoundBarleyMolecular Biology030304 developmental biology0303 health sciencesOligonucleotideChemistryGeneral Neurosciencelcsh:R030302 biochemistry & molecular biologyStructural geneCell BiologyGenomicsGeneral MedicineNuclear matrixG-quadruplexesChromatinBiochemistryGeneral Agricultural and Biological SciencesDNAPeerJ
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Novel atrazine-binding biomimetics inspired to the D1 protein from the photosystem II of Chlamydomonas reinhardtii.

2020

Biomimetic design represents an emerging field for improving knowledge of natural molecules, as well as to project novel artificial tools with specific functions for biosensing. Effective strategies have been exploited to design artificial bioreceptors, taking inspiration from complex supramolecular assemblies. Among them, size-minimization strategy sounds promising to provide bioreceptors with tuned sensitivity, stability, and selectivity, through the ad hoc manipulation of chemical species at the molecular scale. Herein, a novel biomimetic peptide enabling herbicide binding was designed bioinspired to the D1 protein of the Photosystem II of the green alga Chlamydomonas reinhardtii. The D1…

Circular dichroismPhotosystem IIProtein ConformationSupramolecular chemistryPlastoquinoneChlamydomonas reinhardtiiPeptide02 engineering and technologyMolecular Dynamics SimulationBiochemistryFluorescence spectroscopy03 medical and health scienceschemistry.chemical_compoundStructural BiologyBiomimeticsAmino Acid SequencePhotosynthesisMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyRational designphotosystem IIPhotosystem II Protein ComplexGeneral Medicine021001 nanoscience & nanotechnologybiology.organism_classificationSpectrometry FluorescencechemistryArtificial peptides Atrazine sensing Rational designBiophysicsThermodynamicsAtrazine0210 nano-technologyPeptidesChlamydomonas reinhardtiiInternational journal of biological macromolecules
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Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat.

2004

The ability of the cytosolic tail of a plant p24 protein to bind COPI and COPII subunits from plant and animal sources in vitro has been examined. We have found that a dihydrophobic motif in the -7,-8 position (relative to the cytosolic carboxy-terminus), which strongly cooperates with a dilysine motif in the -3,-4 position for COPI binding, is required for COPII binding. In addition, we show that COPI and COPII coat proteins from plant cytosol compete for binding to the sorting motifs in these tails. Only in the absence of the dilysine motif in the -3,-4 position or after COPI depletion could we observe COPII binding to the p24 tail. This competition is not observed when using rat liver cy…

CoatPhysiologyAmino Acid MotifsArabidopsisReceptors Cytoplasmic and NuclearPlant ScienceBiologyCoat Protein Complex ICytosolAnimalsCOPIIBinding SitesVesicular-tubular clusterArabidopsis ProteinsCell BiologyGeneral MedicineCOPIPlant cellIn vitroPeptide FragmentsCell biologyRatsCytosolProtein TransportRat liverCOP-Coated VesiclesProtein BindingSignal TransductionPlantcell physiology
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Structure of mammalian plasma fetuin-B and its mechanism of selective metallopeptidase inhibition

2018

The co-crystal structure of the metallopeptidase astacin with its specific protein inhibitor fetuin-B reveals a novel mechanism of inhibition.

Crystallographymammalian fertilizationmetallopeptidaseResearch Papersstructure determination570 Life sciencesenzyme mechanismsprotein inhibitorQD901-999multi-protein complexessperm–egg fusionpolyspermyprotein structureX-ray crystallography570 Biowissenschaften
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