Search results for "Membrane lipids"

showing 10 items of 80 documents

Human tRNA(Sec) associates with HeLa membranes, cell lipid liposomes, and synthetic lipid bilayers.

2012

We have shown previously that simple RNA structures bind pure phospholipid liposomes. However, binding of bona fide cellular RNAs under physiological ionic conditions is shown here for the first time. Human tRNASec contains a hydrophobic anticodon-loop modification: N6-isopentenyladenosine (i6A) adjacent to its anticodon. Using a highly specific double-probe hybridization assay, we show mature human tRNASec specifically retained in HeLa intermediate-density membranes. Further, isolated human tRNASec rebinds to liposomes from isolated HeLa membrane lipids, to a much greater extent than an unmodified tRNASec transcript. To better define this affinity, experiments with pure lipids show that li…

Membrane lipidsLipid BilayersMolecular Sequence DataPhospholipidBiologyArticlechemistry.chemical_compoundMembrane MicrodomainsSphingosineHumansLipid bilayerMolecular BiologyLipid raftLiposomeMembranesSphingosineBase SequenceRNARNA Transfer Amino Acid-SpecificKineticsMembranechemistryBiochemistryLiposomesNucleic Acid ConformationHydrophobic and Hydrophilic InteractionsHeLa CellsRNA (New York, N.Y.)
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Active Fragments from Pro- and Antiapoptotic BCL-2 Proteins Have Distinct Membrane Behavior Reflecting Their Functional Divergence

2010

International audience; BACKGROUND:The BCL-2 family of proteins includes pro- and antiapoptotic members acting by controlling the permeabilization of mitochondria. Although the association of these proteins with the outer mitochondrial membrane is crucial for their function, little is known about the characteristics of this interaction.METHODOLOGY/PRINCIPAL FINDINGS:Here, we followed a reductionist approach to clarify to what extent membrane-active regions of homologous BCL-2 family proteins contribute to their functional divergence. Using isolated mitochondria as well as model lipid Langmuir monolayers coupled with Brewster Angle Microscopy, we explored systematically and comparatively the…

Membrane lipidsLipid BilayersMolecular Sequence Databcl-X Proteinlcsh:MedicineApoptosisBiologyCell LineProtein–protein interactionMembrane LipidsMice03 medical and health sciences0302 clinical medicineProtein structureMembrane activityAnimalsHumansAmino Acid Sequence[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]lcsh:ScienceLipid bilayerInner mitochondrial membranebcl-2-Associated X Protein030304 developmental biologyMice KnockoutMicroscopy0303 health sciencesMultidisciplinarySequence Homology Amino Acidlcsh:RCytochromes cCell Biology/Cellular Death and Stress ResponsesFibroblastsPeptide FragmentsMitochondriaCell biologyBiochemistry/Molecular EvolutionMembrane proteinBiophysics/Membrane Proteins and Energy Transductionlcsh:QHydrophobic and Hydrophilic Interactions030217 neurology & neurosurgeryFunctional divergenceResearch ArticleBH3 Interacting Domain Death Agonist ProteinProtein BindingPLoS ONE
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Protective effect of melatonin against cytotoxic actions of malondialdehyde: an in vitro study on human erythrocytes

2002

Malondialdehyde (MDA), a by-product of the oxidation of polyunsaturated fatty acids, is strongly cytotoxic. Here we report the in vitro ability of melatonin to protect intact human erythrocytes against the damage induced by the exposure to MDA. MDA at 20 microM caused marked variations in the red blood cell (RBC) membrane. High molecular weight fluorescent adducts were formed within minutes with membrane proteins. A 6-hr incubation led to the oxidation of membrane lipids, as reflected by the formation of conjugated diene (CD) lipid hydroperoxides and oxidation of vitamin E, and to an increase of the high molecular weight fluorescent adducts, which were an indication of MDA finally generated…

Membrane lipidsVitamin Emedicine.medical_treatmentErythrocyte fragilityBiologyMalondialdehydeMelatoninchemistry.chemical_compoundRed blood cellEndocrinologymedicine.anatomical_structureBiochemistrychemistryLipid oxidationMembrane proteinmedicinemedicine.drugJournal of Pineal Research
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Unsaturated fatty acids from food and in the growth medium improve growth of Bacillus cereus under cold and anaerobic conditions.

2013

International audience; In a chemically defined medium and in Luria broth, cold strongly reduced maximal population density of Bacillus cereus ATCC 14579 in anaerobiosis and caused formation of filaments. In cooked spinach, maximal population density of B. cereus in anaerobiosis was the same at cold and optimal temperatures, with normal cell divisions. The lipid containing fraction of spinach, but not the hydrophilic fraction, restored growth of B. cereus under cold and anaerobiosis when added to the chemically defined medium. This fraction was rich in unsaturated, low melting point fatty acids. Addition of phosphatidylcholine containing unsaturated, low melting point, fatty acids similarly…

Membrane lipids[SDV]Life Sciences [q-bio]Bacillus cereusMicrobiology03 medical and health scienceschemistry.chemical_compoundBacillus cereusSpinacia oleraceaPhosphatidylcholineFood scienceAnaerobiosis030304 developmental biology2. Zero hungerchemistry.chemical_classification0303 health sciencesGrowth mediumbiology[ SDV ] Life Sciences [q-bio]030306 microbiologyfungiMembraneFatty acidbiology.organism_classificationFatty acidCulture MediaCold TemperatureChemically defined mediumCereuschemistryBiochemistryFatty Acids UnsaturatedFood MicrobiologySpinachFood ScienceCold
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Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol

1997

Annexin II is an abundant protein which is present in the cytosol and on the cytoplasmic face of plasma membrane and early endosomes. It is generally believed that this association occurs via Ca(2+)-dependent binding to lipids, a mechanism typical for the annexin protein family. Although previous studies have shown that annexin II is involved in early endosome dynamics and organization, the precise biological role of the protein is unknown. In this study, we found that approximately 50% of the total cellular annexin was associated with membranes in a Ca(2+)-independent manner. This binding was extremely tight, since it resisted high salt and, to some extent, high pH treatments. We found, h…

Membrane lipidsmacromolecular substancesBiologyKidneyCell Linechemistry.chemical_compoundMembrane LipidsDogsAnnexinCricetinaeAnimalsCytoskeletonMolecular BiologyAnnexin A2Horseradish PeroxidaseCell MembraneCortical actin cytoskeletonMembrane ProteinsCell BiologyActin cytoskeletonAvidinCell biologyCytoskeletal ProteinsDigitoninCholesterolMembrane proteinchemistryddc:540CalciumAnnexin A2Research ArticleSubcellular Fractions
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Role of Membrane Lipids for the Activity of Pore Forming Peptides and Proteins

2010

Bilayer lipids, far from being passive elements, have multiple roles in polypeptide-dependent pore formation. Lipids participate at all stages of the formation of pores by providing the binding site for proteins and peptides, conditioning their active structure and modulating the molecular reorganization of the membrane complex. Such general functions of lipids superimpose to other particular roles, from electrostatic and curvature effects to more specific actions in cases like cholesterol, sphingolipids or cardiolipin.

Membrane proteinChemistryMembrane lipidsPeripheral membrane proteinMembrane fluiditylipids (amino acids peptides and proteins)Biological membraneLipid bilayerIntegral membrane proteinElasticity of cell membranesCell biology
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Untargeted Metabolomics Investigation on Selenite Reduction to Elemental Selenium by Bacillus mycoides SeITE01

2021

Bacillus mycoides SeITE01 is an environmental isolate that transforms the oxyanion selenite (SeO32−) into the less bioavailable elemental selenium (Se0) forming biogenic selenium nanoparticles (Bio-SeNPs). In the present study, the reduction of sodium selenite (Na2SeO3) by SeITE01 strain and the effect of SeO32− exposure on the bacterial cells was examined through untargeted metabolomics. A time-course approach was used to monitor both cell pellet and cell free spent medium (referred as intracellular and extracellular, respectively) metabolites in SeITE01 cells treated or not with SeO32−. The results show substantial biochemical changes in SeITE01 cells when exposed to SeO32−. The initial u…

Microbiology (medical)Cell signalingMembrane lipidsBacillus mycoides SeITE01 selenite selenium nanoparticles signaling molecules time course untargeted metabolomicschemistry.chemical_elementSettore BIO/19 - Microbiologia GeneraleMicrobiologychemistry.chemical_compoundselenium nanoparticlesExtracellularBacillus mycoides SeITE01time courseSettore CHIM/02 - Chimica Fisicachemistry.chemical_classificationbiologyGlutathioneBacillus mycoidesbiology.organism_classificationQR1-502Amino aciduntargeted metabolomicschemistryBiochemistrysignaling moleculesseleniteSeleniumIntracellular
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Revisiting Plant Plasma Membrane Lipids in Tobacco: A Focus on Sphingolipids

2016

International audience; The lipid composition of plasma membrane (PM) and the corresponding detergent-insoluble membrane (DIM) fraction were analyzed with a specific focus on highly polar sphingolipids, so-called glycosyl inositol phosphorylceramides (GIPCs). Using tobacco (Nicotiana tabacum) 'Bright Yellow 2' cell suspension and leaves, evidence is provided that GIPCs represent up to 40 mol % of the PM lipids. Comparative analysis of DIMs with the PM showed an enrichment of 2-hydroxylated very-long-chain fatty acid-containing GIPCs and polyglycosylated GIPCs in the DIMs. Purified antibodies raised against these GIPCs were further used for immunogold-electron microscopy strategy, revealing …

Models Molecular0106 biological sciences0301 basic medicinePhysiology[SDV]Life Sciences [q-bio]Membrane lipidsNicotiana tabacumCell Culture TechniquesMembrane biologymacromolecular substancesPlant ScienceBiology01 natural sciencesGlycosphingolipidsCell membraneMembrane Lipids03 medical and health scienceschemistry.chemical_compoundMembrane MicrodomainsTobaccoGeneticsmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyInositolGlycosylcardiovascular diseasesSphingolipidsMicroscopy ConfocalCell MembraneFatty Acidstechnology industry and agriculturePhytosterolsArticlesRaftbiology.organism_classificationSphingolipidPlant Leaves030104 developmental biologymedicine.anatomical_structureBiochemistrychemistry[SDE]Environmental Sciencescardiovascular systemlipids (amino acids peptides and proteins)010606 plant biology & botanyPlant Physiology
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Functional competition within a membrane: Lipid recognition vs. transmembrane helix oligomerization

2015

Abstract Binding of specific lipids to large, polytopic membrane proteins is well described, and it is clear that such lipids are crucial for protein stability and activity. In contrast, binding of defined lipid species to individual transmembrane helices and regulation of transmembrane helix monomer–oligomer equilibria by binding of distinct lipids is a concept, which has emerged only lately. Lipids bind to single-span membrane proteins, both in the juxta-membrane region as well as in the hydrophobic membrane core. While some interactions counteract transmembrane helix oligomerization, in other cases lipid binding appears to enhance oligomerization. As reversible oligomerization is involve…

Models MolecularSyntaxin 1AMembrane lipidsLipid BilayersBiophysicsBiologyBinding CompetitiveBiochemistryProtein Structure SecondaryMembrane LipidsLipid bindingOligomerizationIntegral membrane proteinC99Transmembrane channelsMolecular StructureMembrane transport proteinCell MembranePeripheral membrane proteinMembrane ProteinsCell Biologyp24Transmembrane proteinProtein Structure TertiaryCell biologyTransmembrane domainMembrane proteinMembrane proteinbiology.proteinlipids (amino acids peptides and proteins)Protein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Formation of irreversibly bound annexin A1 protein domains on POPC/POPS solid supported membranes

2008

AbstractThe specific interaction of annexin A1 with phospholipid bilayers is scrutinized by means of scanning force and fluorescence microscopy, quartz crystal microbalance, ellipsometry, and modeled by dynamic Monte Carlo simulations. It was found that POPC/POPS bilayers exhibit phase separation in POPC- and POPS-enriched domains as a function of Ca2+ concentration. Annexin A1 interacts with POPC/POPS bilayers by forming irreversibly bound protein domains with monolayer thickness on POPS-enriched nanodomains, while the attachment of proteins to the POPC-enriched regions is fully reversible. A thorough kinetic analysis of the process reveals that both, the binding constant of annexin A1 at …

Models Moleculargenetic structuresLipid BilayersBiophysicsPhospholipidAnalytical chemistryPhosphatidylserines02 engineering and technologyMicroscopy Atomic ForceBiochemistryBiophysical PhenomenaMembrane Lipids03 medical and health scienceschemistry.chemical_compoundProtein structureSFMMonolayerMicropatterned membranesAnimalsHumansPOPCMonte Carlo simulationAnnexin A1030304 developmental biologyFluorescence microscopy0303 health sciencesEllipsometrytechnology industry and agricultureCell BiologyQuartz crystal microbalanceSurface Plasmon Resonance021001 nanoscience & nanotechnologyBinding constantProtein Structure TertiaryMembraneMicroscopy FluorescencechemistryQCMPhosphatidylcholinesBiophysicsCalciumlipids (amino acids peptides and proteins)Adsorption0210 nano-technologyMonte Carlo MethodProtein BindingAnnexin A1Biochimica et Biophysica Acta (BBA) - Biomembranes
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