Search results for "Inner membrane"

showing 9 items of 19 documents

Permeabilization of the Outer Mitochondrial Membrane by Bcl-2 Proteins

2010

The proteins of the Bcl-2 family regulate the release of the apoptotic factors from mitochondria during apoptosis, a key event in physiological cell death. Although their molecular mechanisms remain unclear, the Bcl-2 proteins have been proposed to directly control the permeability of the outer mitochondrial membrane by pore formation. Indeed, they share structural features with the pore forming domains of some bacterial toxins and they can give rise to proteolipidic pores in model membranes. The complex level of regulation needed to decide the fate of the cell is achieved by an intricate interaction network between different members of the family. Current models consider multiple parallel …

Mitochondrial membrane transport proteinMembranebiologyTranslocase of the outer membraneBcl-2 familyTranslocase of the inner membranebiology.proteinMitochondrionMitochondrial carrierBacterial outer membraneCell biology
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Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane.

2000

We have studied the membrane insertion of ProW, an Escherichia coli inner membrane protein with seven transmembrane segments and a large periplasmic N-terminal tail, into endoplasmic reticulum (ER)-derived dog pancreas microsomes. Strikingly, significant levels of N-tail translocation is seen only when a minimum of four of the transmembrane segments are present; for constructs with fewer transmembrane segments, the N-tail remains mostly nontranslocated and the majority of the molecules adopt an 'inverted' topology where normally nontranslocated parts are translocated and vice versa. N-tail translocation can also be promoted by shortening of the N-tail and by the addition of positively charg…

Models MolecularBioquímicaGlycosylationChromosomal translocationBiologyEndoplasmic ReticulumBiochemistryBacterial ProteinsMembranes (Biologia)MicrosomesEscherichia coliAnimalsInner membranePancreasMolecular BiologyEscherichia coli ProteinsEndoplasmic reticulumMembrane ProteinsSTIM1Periplasmic spaceCell BiologyMolecular biologyTransmembrane proteinCell biologyMembrane proteinMutationCatsMicrosomeATP-Binding Cassette TransportersProteïnesJournal of Biological Chemistry
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Crystal structure of the N-terminal domain of the major virulence factor BB0323 from the Lyme disease agent Borrelia burgdorferi.

2019

Lyme disease is an infection caused by the spirochete Borrelia burgdorferi after it is transmitted to a mammalian organism during a tick blood meal. B. burgdorferi encodes at least 140 lipoproteins located on the outer or inner membrane, thus facing the surroundings or the periplasmic space, respectively. However, most of the predicted lipoproteins are of unknown function, and only a few proteins are known to be essential for the persistence and virulence of the pathogen. One such protein is the periplasmic BB0323, which is indispensable for B. burgdorferi to cause Lyme disease and the function of which is associated with cell fission and outer membrane integrity. After expression and trans…

Models MolecularLyme DiseaseVirulence FactorsLipoproteinsVirulencePeriplasmic spaceBiologybiology.organism_classificationVirulence factorCell biologyBacterial ProteinsStructural BiologyBorrelia burgdorferiInner membraneSpectrinAmino Acid SequenceBorrelia burgdorferiBacterial outer membranePathogenActa crystallographica. Section D, Structural biology
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Neurochemical and morphological studies on demyelination in multiple sclerosis with special reference to etiological aspects.

1972

Light microscopic studies were used as control for neurochemical studies and these showed that some micro plaques could be found also in areas which were normal on visual inspection. Also foreign cell infiltrates were found outside any clear plaque material. The number of these cells did not correlate with other findings like lipid or enzyme chemistry. In electronmicroscopic studies astrocytes demonstrated most lysosomes and phagocytosis of myelin. This increased lysosomal reaction was demonstrated also in biochemical analyses performed on MS biopsy specimens. Occasional nuclear changes like inclusion bodies and protrusion of inner nuclear membrane were observed suggesting some exogenous, p…

Pathologymedicine.medical_specialtyMultiple SclerosisGlycoside HydrolasesBiopsyAcid PhosphataseBiologyInclusion bodiesMyelinNeurochemicalPhagocytosismedicineInner membraneHumansMyelin SheathGlucuronidaseCell NucleusInclusion BodiesMembranesMultiple sclerosisEsterasesLipid metabolismmedicine.diseaseLipid MetabolismAxonsPhosphoric Monoester HydrolasesCell nucleusMicroscopy Electronmedicine.anatomical_structureNeurologyNeurogliaNeurology (clinical)AutopsyLysosomesNeurogliaPeptide HydrolasesZeitschrift fur Neurologie
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Study of Bacillus subtilis spore's : characterication of stuctures implied in its resistance

2013

The bacterial spore is a multilayer microbial form which is extremely resistant to environmental perturbations. This resistance is especially due to its unique structure which is particularly compact and weakly permeable. This work aims to identify and characterize the spore structures involved in these properties. Overall investigation methods, such as NMR and fluorescence anisotropy, have shown that the cortex of Bacillus subtilis spores is modified by temperature for level similar to that of the activation of germination. This will result in changes to the access to the inner membrane. A tool at the spore’s scale, the fluorescence lifetime imaging microscopy (FLIM) in conjunction with th…

Spores de Bacillus subtilisEthanolMembrane interneCortexInner membraneBacillus subtilis sporesImagerie en temps de vie de fluorescence[SDV.MP.BAC] Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyFluorescence lifetime imaging[SDV.BIO] Life Sciences [q-bio]/Biotechnology
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Insertion of a malE B-Galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processin…

1982

The synthesis of a membrane-bound MalE ,B-galactosidase hybrid protein, when induced by growth of Escherichia coli on maltose, leads to inhibition of cell division and eventually a reduced rate of mass increase. In addition, the relative rate of synthesis of outer membrane proteins, but not that of inner membrane proteins, was reduced by about 50%o. Kinetic experiments demonstrated that this reduction coincided with the period of maximum synthesis of the hybrid protein (and another maltose-inducible protein, LamB). The accumulation of this abnormal protein in the envelope therefore appeared specifically to inhibit the synthesis, the assembly of outer membrane proteins, or both, indicating t…

Vesicle-associated membrane protein 8MembranesPeripheral membrane proteinDNA RecombinantMembrane ProteinsPorinsBiologyMicrobiologyCell biologyTransport proteinKineticsEscheríchia coliBacterial ProteinsMembrane proteinEscherichia coliReceptors VirusOuter membrane efflux proteinsInner membraneProtein PrecursorsMaltoseBacterial outer membraneMolecular BiologyIntegral membrane proteinProteïnesBacterial Outer Membrane Proteins
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Probing protein interactions in the membrane-containing virus PRD1.

2015

PRD1 is a Gram-negative bacteria infecting complex tailless icosahedral virus with an inner membrane. This type virus of the family Tectiviridae contains at least 18 structural protein species, of which several are membrane associated. Vertices of the PRD1 virion consist of complexes recognizing the host cell, except for one special vertex through which the genome is packaged. Despite extensive knowledge of the overall structure of the PRD1 virion and several individual proteins at the atomic level, the locations and interactions of various integral membrane proteins and membrane-associated proteins still remain a mystery. Here, we demonstrated that blue native PAGE can be used to probe pro…

Viral Structural Proteins0303 health sciencesVesicle-associated membrane protein 8Macromolecular Substances030302 biochemistry & molecular biologyMutantMembrane ProteinsBiologyVirologyTransmembrane proteinProtein–protein interaction03 medical and health sciencesLytic cycleVirologyProtein Interaction MappingInner membraneTectiviridaeBacteriophage PRD1Electrophoresis Polyacrylamide GelProtein MultimerizationIntegral membrane protein030304 developmental biologyThe Journal of general virology
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Fluorenylmethoxycarbonyl-N-methylamino Acids Synthesized in a Flow Tube-in-Tube Reactor with a Liquid-Liquid Semipermeable Membrane

2013

Both steps of the N-methylation of 9-fluorenylmethoxycarbonyl (Fmoc) amino acids were carried out in a microstructured tube-in-tube reactor equipped with a semipermeable Teflon® AF 2400 membrane as the inner tubing. In the first step, gaseous formaldehyde was passed through the inner membrane to effect the acid-catalyzed conversion of the Fmoc amino acids into the corresponding N-Fmoc oxazolidinones. In the second step, liquid–liquid transfer of trifluoroacetic acid was used for the first time in such a reactor for the reductive opening of these oxazolidinones to give Fmoc N-methylamino acids in high yields.

chemistry.chemical_classificationChromatographyChemistryOrganic ChemistryFlow chemistryAmino acidchemistry.chemical_compoundMembraneTrifluoroacetic acidLiquid liquidInner membraneOrganic chemistrySemipermeable membranePhysical and Theoretical ChemistryMicroreactorEuropean Journal of Organic Chemistry
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Genetic Systems for Monitoring Interactions of Transmembrane Domains in Bacterial Membranes

2013

In recent years several systems have been developed to study interactions of TM domains within the inner membrane of the Gram-negative bacterium Escherichia coli. Mostly, a transmembrane domain of interest is fused to a soluble DNA-binding domain, which dimerizes in E. coli cytoplasm after interactions of the transmembrane domains. The dimeric DNA-binding domain subsequently binds to a promoter/operator region and thereby activates or represses a reporter gene. In 1996 the first bacterial system has been introduced to measure interactions of TM helices within a bacterial membrane, which is based on fusion of a transmembrane helix of interest to the DNA-binding domain of the Vibrio cholerae …

chemistry.chemical_compoundTransmembrane domainReporter geneOperator (biology)chemistryCytoplasmmedicineBiophysicsInner membranemedicine.disease_causeEscherichia coliDNADomain (software engineering)
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