Search results for "Membrane Lipids"

showing 10 items of 80 documents

Mechanisms of RNA loading into exosomes

2015

AbstractUpon fusion of multivesicular bodies (MVBs) with the plasma membrane, intraluminal vesicles (ILVs) are released into the extracellular space as exosomes. Since the lipid composition of the exosomal membrane resembles that of raft microdomains, the inward budding process involves the raft-like region of the MVB limiting membrane. Although published research suggests that cellular RNAs may be selectively sorted into exosomes, the molecular mechanisms remain elusive. In this review, we suggest that there is a continuous interaction of cellular RNAs with the outer (cytoplasmic) surface of MVBs and that the selection for incorporation of these RNAs into ILVs is based on their affinity to…

CeramideBiophysicsBiologyExosomesModels BiologicalBiochemistryIntraluminal vesiclesCeramideMembrane Lipidschemistry.chemical_compoundRaftsMembrane MicrodomainsStructural BiologymicroRNAGeneticsExtracellularAnimalsHumansMolecular BiologyVesicleCell MembraneMembraneMultivesicular BodiesRNA-Binding ProteinsRNAMicroRNACell BiologyRaftMicrovesiclesCell biologychemistryCytoplasmRNAlipids (amino acids peptides and proteins)FEBS Letters
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Polymerization in black lipid membranes. Influence on ion transport

1986

A variety of different lipids containing dienoyl groups in the side chains were tested for membrane formation using the planar lipid bilayer approach. One of these lipids formed stable bilayers which could be polymerized using UV-illumination. The influence of the polymerization was studied in monolayers, lipid vesicles and planar bilayers. The stability of the lipid bilayer membranes was increased by polymerization. Thus, the lifetime of the membranes increased from about 1 h to 4–5 h or longer. Furthermore, the specific conductance of unmodified membranes and of carrier-mediated transport is reduced. The transport of lipophilic ions was investigated as a function of polymerization using t…

ChemistryMembrane lipidstechnology industry and agricultureBiophysicsBiological membraneGeneral MedicineModel lipid bilayerMembranePolymerizationMembrane fluidityBiophysicsOrganic chemistryLipid bilayer phase behaviorLipid bilayer
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How copper ions and membrane environment influence the structure of the human and chicken tandem repeats domain?

2019

Abstract Prion proteins (PrPs) from different species have the enormous ability to anchor copper ions. The N-terminal domain of human prion protein (hPrP) contains four tandem repeats of the –PHGGGWGQ– octapeptide sequence. This octarepeat domain can bind up to four Cu2+ ions. Similarly to hPrP, chicken prion protein (chPrP) is able to interact with Cu2+ through the tandem hexapeptide -HNPGYP- region (residues 53–94). In this work, we focused on the human octapeptide repeat (human Octa4, hPrP60–91) (Ac-PHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQ-NH2) and chicken hexapeptide repeat (chicken Hexa4, chPrP54–77) (Ac-HNPGYPHNPGYPHNPGYPHNPGYP-NH2) prion protein fragments. Due to the fact that PrP is a membr…

Circular dichroism010402 general chemistry01 natural sciencesBiochemistryMicelleInorganic Chemistrychemistry.chemical_compoundMembrane LipidsTandem repeatPeptide bondAnimalsHumansAmino Acid SequenceSodium dodecyl sulfateLipid bilayerMembrane mimicking environmentMicelleschemistry.chemical_classification010405 organic chemistryChemistryCopper ionsSodium Dodecyl SulfateHistidine residues0104 chemical sciencesPrion proteinsMembraneTandem Repeat SequencesBiophysicsPotentiometryThermodynamicsGlycoproteinChickensCopper
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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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Size-exclusion high-performance liquid chromatography in the study of the autoassociating antibiotic gramicidin A in micellar milieu.

2003

Gramicidin A (gA) is a polypeptide antibiotic which forms dimeric channels specific for monovalent cations in biological membranes. It is a polymorphic molecule that adopts several different conformations, double-stranded (ds) helical dimers (pore conformation) and single-stranded beta-helical dimers (channel conformation). This study investigated the conformational adaptability of gramicidin A when incorporated into micelles as membrane-mimetic model system. Taking advantage of our reported, versatile, size-exclusion high-performance liquid chromatography (SE-HPLC) strategy that allows the separation of double-stranded dimers and monomers, we have quantitatively characterized the conformat…

Circular dichroismStereochemistryProtein ConformationSize-exclusion chromatographyBiophysicsPeptideBiochemistryMicellechemistry.chemical_compoundMembrane LipidsSurface-Active AgentsProtein structureBiomimetic MaterialsColloidsChromatography High Pressure LiquidMicelleschemistry.chemical_classificationCircular DichroismGramicidinBiological membraneMembranes ArtificialCombinatorial chemistryAnti-Bacterial AgentsMembraneMonomerchemistryChromatography GelDimerizationJournal of biochemical and biophysical methods
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Staphylococcal α-toxin: the role of the N-terminus in formation of the heptameric pore — a fluorescence study1This work contains parts of the M.D. th…

1997

Staphylococcus aureus alpha-toxin forms heptameric pores on eukaryotic cell membranes. Assembly of the heptamer precedes formation of the transmembrane pore. The latter event depends on a conformational change that drives a centrally located stretch of 15 amino acid residues into the lipid bilayer. A second region of the molecule that has been implicated in the pre-pore to pore transition is the far N-terminus. Here, we used fluorescently labeled single cysteine replacement mutants to analyze the functional role of the far N-terminus of alpha-toxin. Pyrene attached to mutants S3C, I5C and 17C forms excimers within the toxin pore complex. This indicates that the distance of adjacent N-termin…

Conformational changePore complexStereochemistryMembrane lipidsBiophysicsCell BiologyN-terminusα-ToxinBiochemistryTransmembrane proteinchemistry.chemical_compoundProtein structureMembranechemistryHeptameric poreBiophysicsPyreneLipid bilayer(Staphylococcus aureus)Biochimica et Biophysica Acta (BBA) - Biomembranes
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Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin.

1996

Staphylococcus aureus alpha-toxin is a hydrophilic polypeptide of 293 amino acids that produces heptameric transmembrane pores. During assembly, the formation of a pre-pore precedes membrane permeabilization; the latter is linked to a conformational change in the oligomer. Here, 41 single-cysteine replacement toxin mutants were thiol-specifically labelled with the polarity-sensitive fluorescent probe acrylodan. After oligomerization on membranes, only the mutants with acrylodan attached to residues in the sequence 118-140 exhibited a marked blue shift in the fluorescence emission maximum, indicative of movement of the fluorophore to a hydrophobic environment. Within this region, two functio…

Conformational changeStaphylococcus aureusProtein ConformationMembrane lipidsBacterial ToxinsMolecular Sequence DataBiologyGeneral Biochemistry Genetics and Molecular BiologyCell membraneHemolysin ProteinsProtein structure2-NaphthylaminemedicinePoint MutationAmino Acid SequenceCysteineMolecular BiologyPeptide sequenceFluorescent Dyeschemistry.chemical_classificationBinding SitesGeneral Immunology and MicrobiologyMolecular StructureGeneral NeuroscienceCell MembraneTransmembrane proteinAmino acidmedicine.anatomical_structureMembraneSpectrometry FluorescenceBiochemistrychemistryLiposomesBiophysicsMutagenesis Site-DirectedResearch ArticleThe EMBO journal
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The Proteome and Lipidome of Synechocystis sp. PCC 6803 Cells Grown under Light-Activated Heterotrophic Conditions*

2015

Cyanobacteria are photoautotrophic prokaryotes with a plant-like photosynthetic machinery. Because of their short generation times, the ease of their genetic manipulation, and the limited size of their genome and proteome, cyanobacteria are popular model organisms for photosynthetic research. Although the principal mechanisms of photosynthesis are well-known, much less is known about the biogenesis of the thylakoid membrane, hosting the components of the photosynthetic, and respiratory electron transport chain in cyanobacteria. Here we present a detailed proteome analysis of the important model and host organism Synechocystis sp. PCC 6803 under light-activated heterotrophic growth condition…

CyanobacteriaProtein FoldingProteomePhotosynthesisThylakoidsBiochemistryMass SpectrometryAnalytical ChemistryRespiratory electron transport chainMembrane LipidsBacterial ProteinsMolecular BiologybiologyResearchSynechocystisLipidomebiology.organism_classificationCarbonOxidative StressPhototrophic ProcessesMembraneBiochemistryThylakoidProteomeBiogenesisChromatography LiquidMolecular & Cellular Proteomics
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Changes in membrane lipid composition in ethanol- and acid-adapted Oenococcus oeni cells: characterization of the cfa gene by heterologous complement…

2008

International audience; Cyclopropane fatty acid (CFA) synthesis was investigated in Oenococcus oeni. The data obtained demonstrated that acid-grown cells or cells harvested in the stationary growth phase showed changes in fatty acid composition similar to those of ethanol-grown cells. An increase of the CFA content and a decrease of the oleic acid content were observed. The biosynthesis of CFAs from unsaturated fatty acid phospholipids is catalysed by CFA synthases. Quantitative real-time-PCR experiments were performed on the cfa gene of O. oeni, which encodes a putative CFA synthase. The level of cfa transcripts increased when cells were harvested in stationary phase and when cells were gr…

CyclopropanesMESH: Hydrogen-Ion ConcentrationTranscription GeneticMESH: Gram-Positive Coccimedicine.disease_causechemistry.chemical_compoundMESH: CyclopropanesCloning MolecularMESH: Bacterial ProteinsOenococcus oeni0303 health sciencesMESH: Gene Expression Regulation BacterialMESH: Genetic Complementation TestbiologyStrain (chemistry)MESH: Escherichia coliFatty AcidsHydrogen-Ion ConcentrationMESH: Fatty AcidsGram-Positive CocciComplementationRNA BacterialBiochemistryMESH: RNA BacterialMESH: EthanolMESH: Sequence AlignmentMicrobiologycomplex mixturesMembrane Lipids03 medical and health sciencesBacterial ProteinsMESH: MethyltransferasesEscherichia colimedicineMESH: Cloning Molecular[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCyclopropane fatty acidEthanol metabolismEscherichia coliUnsaturated fatty acid030304 developmental biologyEthanol030306 microbiologyMESH: Transcription GeneticGenetic Complementation TestMESH: Oleic AcidGene Expression Regulation BacterialMethyltransferasesbiology.organism_classificationOleic acidchemistryMESH: Membrane LipidsSequence AlignmentOleic Acid
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Cyclopropanation of Membrane Unsaturated Fatty Acids Is Not Essential to the Acid Stress Response of Lactococcus lactis subsp. cremoris

2011

ABSTRACT Cyclopropane fatty acids (CFAs) are synthetized in situ by the transfer of a methylene group from S -adenosyl- l -methionine to a double bond of unsaturated fatty acid chains of membrane phospholipids. This conversion, catalyzed by the Cfa synthase enzyme, occurs in many bacteria and is recognized to play a key role in the adaptation of bacteria in response to a drastic perturbation of the environment. The role of CFAs in the acid tolerance response was investigated in the lactic acid bacterium Lactococcus lactis MG1363. A mutant of the cfa gene was constructed by allelic exchange. The cfa gene encoding the Cfa synthase was cloned and introduced into the mutant to obtain the comple…

CyclopropanesPhysiologyMembrane lipidsMutantApplied Microbiology and BiotechnologyGas Chromatography-Mass SpectrometryMembrane LipidsStress PhysiologicalMembrane fluidityViability assayPhospholipidsUnsaturated fatty acidMicrobial ViabilityEcologybiologyLactococcus lactis subsp cremorisFatty AcidsGenetic Complementation TestLactococcus lactisMethyltransferasesbiology.organism_classificationLactococcus lactisBiochemistryFatty Acids UnsaturatedMutant ProteinsAcidsBacteriaFood ScienceBiotechnologyApplied and Environmental Microbiology
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