Search results for "Membrana"

showing 10 items of 91 documents

The Plant Inorganic Pyrophosphatase Does Not Transport K+ in Vacuole Membrane Vesicles Multilabeled with Fluorescent Probes for H+, K+, and Membrane …

1995

Abstract It has been claimed that the inorganic pyrophosphatase (PPase) of the plant vacuolar membrane transports K+ in addition to H+ in intact vacuoles (Davies, J. M., Poole, R. J., Rea, P. A., and Sanders, D.(1992) Proc. Natl. Acad. Sci. U. S. A. 89, 11701-11705). Since this was not confirmed using the purified and reconstituted PPase consisting of a 75-kDa polypeptide (Sato, M. H., Kasahara, M., Ishii, N., Homareda, H., Matsui, H., and Yoshida, M. (1994) J. Biol. Chem. 269, 6725-6728), these authors proposed that K+ transport by the PPase is dependent on its association with other membrane components lost during purification. We have examined the hypothesis of K+ translocation by the PP…

0106 biological sciencespyrophosphataseProtonophoreIonophoreVacuole01 natural sciencesBiochemistryPyrophosphateMembrane Potentials03 medical and health scienceschemistry.chemical_compoundValinomycinvitis viniferahydrolyseion potassiumtransport membranaire[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]PyrophosphatasesMolecular BiologyComputingMilieux_MISCELLANEOUSFluorescent Dyes030304 developmental biologyionophoreMembrane potential0303 health sciencesInorganic pyrophosphatasemembrane vacuolaireIon TransportVesicleIntracellular MembranesCell BiologyPlantsEnzyme ActivationInorganic PyrophosphataseBiochemistrychemistrypotentiel membranaireVacuolesPotassiumBiophysicsProtonsvigneHydrogen010606 plant biology & botanyJournal of Biological Chemistry
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NMR Investigation of Structures of G-Protein Coupled Receptor Folding Intermediates

2016

Folding of G-protein coupled receptors (GPCRs) according to the two-stage model (Popot, J. L., and Engelman, D. M. (1990) Biochemistry 29, 4031-4037) is postulated to proceed in 2 steps: partitioning of the polypeptide into the membrane followed by diffusion until native contacts are formed. Herein we investigate conformational preferences of fragments of the yeast Ste2p receptor using NMR. Constructs comprising the first, the first two, and the first three transmembrane (TM) segments, as well as a construct comprising TM1-TM2 covalently linked to TM7 were examined. We observed that the isolated TM1 does not form a stable helix nor does it integrate well into the micelle. TM1 is significant…

0301 basic medicine10120 Department of ChemistryBioquímicaSaccharomyces cerevisiae Proteins1303 BiochemistryProtein ConformationStereochemistrySaccharomyces cerevisiaeBiochemistryMicelleRessonància magnètica nuclear1307 Cell BiologyG03 medical and health sciencesprotein coupled receptorGPCRProtein Domains540 Chemistry1312 Molecular BiologyAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyMicellesG protein-coupled receptorSequence Homology Amino Acid030102 biochemistry & molecular biologyChemistryProteïnes de membranaFoldingCell BiologyTransloconPeptide FragmentsTransmembrane proteinNMRFolding (chemistry)Crystallography030104 developmental biologyStructural biology10036 Medical ClinicProtein Structure and FoldingReceptors Mating FactorHelixProtein folding
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Human peroxin PEX3 is co-translationally integrated into the ER and exits the ER in budding vesicles

2015

The long-standing paradigm that all peroxisomal proteins are imported post-translationally into pre-existing peroxisomes has been challenged by the detection of peroxisomal membrane proteins (PMPs) inside the endoplasmic reticulum (ER). In mammals, the mechanisms of ER entry and exit of PMPs are completely unknown. We show that the human PMP PEX3 inserts co-translationally into the mammalian ER via the Sec61 translocon. Photocrosslinking and fluorescence spectroscopy studies demonstrate that the N-terminal transmembrane segment (TMS) of ribosome-bound PEX3 is recognized by the signal recognition particle (SRP). Binding to SRP is a prerequisite for targeting of the PEX3-containing ribosome•n…

0301 basic medicineLipoproteinsPeroxinBiologyEndoplasmic ReticulumBiochemistryenvironment and public healthPeroxins03 medical and health sciencesStructural BiologyGeneticsPeroxisomesHumansMolecular BiologySignal recognition particle receptorAdaptor Proteins Signal TransducingSec61 transloconSignal recognition particlebudding vesiclesEndoplasmic reticulumCèl·lules eucarioteshuman peroxisomal membrane protein PEX3Proteïnes de membranaMembrane ProteinsCell BiologyOriginal ArticlesIntracellular MembranesTransloconSEC61 TransloconTransport proteinCell biologyperoxisomal biogenesisProtein Transport030104 developmental biologyMembrane proteinOriginal ArticleRibosomesSignal Recognition Particle
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Characterization of the inner membrane protein BB0173 from Borrelia burgdorferi.

2017

Abstract Background The bacterial spirochete Borrelia burgdorferi is the causative agent of the most commonly reported arthropod-borne illness in the United States, Lyme disease. A family of proteins containing von Willebrand Factor A (VWFA) domains adjacent to a MoxR AAA+ ATPase have been found to be highly conserved in the genus Borrelia. Previously, a VWFA domain containing protein of B. burgdorferi, BB0172, was determined to be an outer membrane protein capable of binding integrin α3β1. In this study, the characterization of a new VWFA domain containing membrane protein, BB0173, is evaluated in order to define the location and topology of this multi-spanning membrane protein. In additio…

0301 basic medicineMicrobiology (medical)Models Molecular030106 microbiologylcsh:QR1-502MicrobiologiaDown-RegulationGene ExpressionBiologyEndoplasmic ReticulumMicrobiologylcsh:MicrobiologyMicrobiology03 medical and health sciencesBacterial ProteinsStress PhysiologicalBorreliaInner membraneAmino Acid SequenceBorrelia burgdorferiAerotoleranceCell MembraneProteïnes de membranaMembrane ProteinsPeriplasmic spacebiology.organism_classificationbacterial infections and mycosesTransmembrane proteinTransmembraneCell biologyOxygenTransmembrane domainMembrane proteinBorrelia burgdorferivonWillebrand factor aMutationPeriplasmBacterial outer membraneSequence AlignmentResearch ArticleMIDAS motifBMC microbiology
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Biological insertion of computationally designed short transmembrane segments

2016

The great majority of helical membrane proteins are inserted co-translationally into the ER membrane through a continuous ribosome-translocon channel. The efficiency of membrane insertion depends on transmembrane (TM) helix amino acid composition, the helix length and the position of the amino acids within the helix. In this work, we conducted a computational analysis of the composition and location of amino acids in transmembrane helices found in membrane proteins of known structure to obtain an extensive set of designed polypeptide segments with naturally occurring amino acid distributions. Then, using an in vitro translation system in the presence of biological membranes, we experimental…

0301 basic medicineModels MolecularBiologyEndoplasmic ReticulumArticleProtein Structure Secondary03 medical and health sciencesOrientations of Proteins in Membranes databaseMembranes (Biologia)Amino Acid SequenceIntegral membrane proteinMultidisciplinary030102 biochemistry & molecular biologyPeripheral membrane proteinCell MembraneProteïnes de membranaComputational BiologyMembrane ProteinsBiological membraneBiofísicaTransmembrane proteinTransmembrane domain030104 developmental biologyBiochemistryMembrane proteinHelixBiophysicsPeptidesScientific Reports
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The C-terminal Domains of Apoptotic BH3-only Proteins Mediate Their Insertion into Distinct Biological Membranes

2016

Changes in the equilibrium of pro- and anti-apoptotic members of the B-cell lymphoma-2 (Bcl-2) protein family in the mitochondrial outer membrane (MOM) induce structural changes that commit cells to apoptosis. Bcl-2 homology-3 (BH3)-only proteins participate in this process by either activating pro-apoptotic effectors or inhibiting anti-apoptotic components and by promoting MOM permeabilization. The association of BH3-only proteins with MOMs is necessary for the activation and amplification of death signals; however, the nature of this association remains controversial, as these proteins lack a canonical transmembrane sequence. Here we used an in vitro expression system to study the inserti…

0301 basic medicineProtein familyCèl·lulesBiologyBiochemistryMitochondrial Proteins03 medical and health sciencesProtein DomainsMembranes (Biologia)Protein-fragment complementation assayMembrane BiologyMicrosomesProto-Oncogene ProteinsHumansMolecular BiologyAdaptor Proteins Signal TransducingGeneticsBcl-2-Like Protein 11030102 biochemistry & molecular biologyCell MembraneBcl-2 familyProteïnes de membranaMembrane ProteinsBiological membraneCell BiologyFusion proteinTransmembrane proteinCell biology030104 developmental biologyMembraneProto-Oncogene Proteins c-bcl-2Membrane proteinB-cell lymphoma 2 (Bcl-2) family BH3-only apoptosis membrane insertion membrane protein mitochondrial apoptosis transmembrane domainApoptosis Regulatory ProteinsHydrophobic and Hydrophilic InteractionsHeLa CellsJournal of Biological Chemistry
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Cellular Injuries in Cronobacter sakazakii CIP 103183T and Salmonella enterica Exposed to Drying and Subsequent Heat Treatment in Milk Powder

2018

International audience; Because of the ability of foodborne pathogens to survive in low-moisture foods, their decontamination is an important issue in food protection. This study aimed to clarify some of the cellular mechanisms involved in inactivation of foodborne pathogens after drying and subsequent heating. Individual strains of Salmonella Typhimurium, Salmonella Senftenberg, and Cronobacter sakazakii were mixed into whole milk powder and dried to different water activity levels (0.25 and 0.58); the number of surviving cells was determined after drying and subsequent thermal treatments in closed vessels at 90 and 100 degrees C, for 30 and 120 s. For each condition, the percentage of unc…

0301 basic medicineSalmonellalcsh:QR1-502medicine.disease_causelcsh:Microbiologyperméabilité membranairechemistry.chemical_compound[SDV.IDA]Life Sciences [q-bio]/Food engineeringFood sciencedryingOriginal Researchpropidium iodidebiologyChemistryMicrobiology and Parasitologyplasma-membraneSalmonella entericainfant formulaMicrobiologie et ParasitologieSalmonella entericaAlimentation et Nutritionsaccharomyces-cerevisiaeenterobacter-sakazakiitraitement thermiqueséchageMicrobiology (medical)Water activityMembrane permeabilitydesiccation tolerance030106 microbiologylow-water activityMicrobiologyrespiratory activity03 medical and health sciencesCronobacter sakazakiimedicineFood and NutritionPropidium iodideactivation respiratoireEscherichia colifoodborne pathogensheat treatmentbiology.organism_classificationCronobacter sakazakii030104 developmental biologymembrane permeabilitythermal inactivationSalmonella enterica;Cronobacter sakazakii;membrane permeability;respiratory activity;heat treatment;dryingescherichia-coliBacteria
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Membrane insertion and topology of the translocon-associated protein (TRAP) gamma subunit

2017

Translocon-associated protein (TRAP) complex is intimately associated with the ER translocon for the insertion or translocation of newly synthesised proteins in eukaryotic cells. The TRAP complex is comprised of three single-spanning and one multiple-spanning subunits. We have investigated the membrane insertion and topology of the multiple-spanning TRAP-γ subunit by glycosylation mapping and green fluorescent protein fusions both in vitro and in cell cultures. Results demonstrate that TRAP-γ has four transmembrane (TM) segments, an Nt/Ct cytosolic orientation and that the less hydrophobic TM segment inserts efficiently into the membrane only in the cellular context of full-length protein.

0301 basic medicineVesicle-associated membrane protein 8Receptors PeptideProtein subunitBiophysicsReceptors Cytoplasmic and NuclearBiologyEndoplasmic ReticulumTopologyBiochemistryGreen fluorescent protein03 medical and health sciencesN-linked glycosylationMembranes (Biologia)Membrane GlycoproteinsEndoplasmic reticulumCalcium-Binding ProteinsProteïnes de membranaMembrane ProteinsCell BiologyTransloconTransmembrane proteinProtein Subunits030104 developmental biologyHydrophobic and Hydrophilic InteractionsGamma subunit
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Biogénesis y plegamiento de proteínas de membrana

2011

Todas las células, ya sean bacterias, arqueas o eucariotas están delimitadas por membranas. Las membranas biológicas están compuestas principalmente por lípidos estructurados en dos monocapas enfrentadas, por lo que también se les denomina bicapas lipídicas. La membrana, además de definir los límites tanto celulares como organulares y establecer una barrera al tráfico de moléculas de unos compartimentos a otros posee otras funciones importantes para la supervivencia celular, como el transporte selectivo, la producción de la mayoría de energía requerida para los procesos catalíticos y la transducción de señales. 618/5000 All cells, whether bacteria, archaea or eukaryotes are bounded by membr…

:QUÍMICA::Química macromolecular [UNESCO]UNESCO::QUÍMICA::Química macromolecularproteínas de membrana
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CARATTERIZZAZIONE E MODELLISTICA DI UNO STACK DI CELLE A MEMBRANA POLIMERICA (PEM) PER SISTEMI DI PROPULSIONE PER AUTOMOTIVE

2011

AUTOMOTIVESettore ING-IND/32 - Convertitori Macchine E Azionamenti ElettriciMEMBRANA POLIMERICA (PEM)
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