Search results for "Inner membrane"

showing 10 items of 19 documents

No exception to the rule: Candidatus Portiera aleyrodidarum cell wall revisited

2014

International audience; Many insect endosymbionts described so far are gram-negative bacteria. Primary endosymbionts are obligatory bacteria usually harboured by insects inside vacuoles in specialized cells called bacteriocytes. This combination produces a typical three-membrane system with one membrane derived from the insect vacuole and the other two from the bacterial gram-negative cell envelope, composed by the cell wall (the outer membrane plus the periplasmic space) and the plasma membrane (the inner membrane). For the last 21 years, the primary endosymbiont of whiteflies 'Candidatus Portiera aleyrodidarum' was considered an exception to this rule. Previous works stated that only two …

0106 biological sciencesGram-negative bacteriacell envelopeCandidatus Carsonella ruddii[SDV]Life Sciences [q-bio]Bemisia tabaci endosymbiont01 natural sciencesMicrobiologyMicrobiologyHemipteraCell membrane03 medical and health sciencesMicroscopy Electron TransmissionCell WallGeneticsmedicineAnimalsInner membraneMolecular Biology030304 developmental biology0303 health sciencesbiologyfungiPeriplasmic spacebiochemical phenomena metabolism and nutritionbiology.organism_classificationHalomonadaceaemedicine.anatomical_structureGenes Bacterialendosymbiont membranesCandidatusbacteriaCell envelopeBacterial outer membrane010606 plant biology & botany
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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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Protoparvovirus Knocking at the Nuclear Door

2017

Protoparvoviruses target the nucleus due to their dependence on the cellular reproduction machinery during the replication and expression of their single-stranded DNA genome. In recent years, our understanding of the multistep process of the capsid nuclear import has improved, and led to the discovery of unique viral nuclear entry strategies. Preceded by endosomal transport, endosomal escape and microtubule-mediated movement to the vicinity of the nuclear envelope, the protoparvoviruses interact with the nuclear pore complexes. The capsids are transported actively across the nuclear pore complexes using nuclear import receptors. The nuclear import is sometimes accompanied by structural chan…

0301 basic medicinevirusesimportinsActive Transport Cell Nucleuslcsh:QR1-502Genome ViralReviewImportinKaryopherinsBiologyVirus Replicationlcsh:MicrobiologyParvovirusMice03 medical and health sciencesCapsidVirologynuclear pore complexmedicineAnimalsHumansInner membraneNuclear poreprotoparvovirusCell Nucleusnuclear localization sequence030102 biochemistry & molecular biologyta1182nuclear envelopeVirus InternalizationVirologynuclear importCell biologyCell nucleusnuclear envelope break down030104 developmental biologyInfectious Diseasesmedicine.anatomical_structureintracellular dynamicsEndosomal transportNuclear PoreentryCapsid ProteinsNucleoporinNuclear transportNuclear localization sequenceViruses
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2020

The transfer of metabolites through the mitochondrial membranes is a vital process that is highly controlled and regulated by the inner membrane. A variety of metabolites, nucleotides, and cofactors are transported across the inner mitochondrial membrane (IMM) by a superfamily of membrane transporters which are known as the mitochondrial carrier family (MCF) or the solute carrier family 25 (SLC25 protein family). In humans, the MCF has 53 members encoded by nuclear genes. Members of the SLC25 family of transporters, which is the largest group of solute carriers, are also known as mitochondrial carriers (MCs). Because MCs are nuclear-coded proteins, they must be imported into the IMM. When c…

0303 health sciencesProtein familyChemistryOrganic ChemistryPharmaceutical ScienceMitochondrionMitochondrial carrierTransmembrane protein3. Good healthAnalytical ChemistrySolute carrier familyCell biology03 medical and health sciences0302 clinical medicineChemistry (miscellaneous)030220 oncology & carcinogenesisDrug DiscoveryCancer cellMolecular MedicineInner membranePhysical and Theoretical ChemistryInner mitochondrial membrane030304 developmental biologyMolecules
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Involvement of the Pseudomonas aeruginosa MexAB–OprM efflux pump in the secretion of the metallophore pseudopaline

2020

ABSTRACTThe ability for all organisms to acquire metals from their environment is essential for life. To overcome the metal restriction imposed by the host’s nutritional immunity, bacterial pathogens exploits the use of small high metal affinity molecules called metallophores. Metallophores are first synthetized in the cytoplasm, then secreted into the medium where they sequester the metal. The metal-metallophore complex is then imported into the bacterium following binding to dedicated cell surface receptors. Recently, a new family of metallophores has been discovered in pathogenic bacteria called staphylopine in Staphylococcus aureus and pseudopaline in Pseudomonas aeruginosa. Here, we ar…

Bodily Secretions[SDV]Life Sciences [q-bio]Microbial Sensitivity TestsBiologymedicine.disease_causeMicrobiology03 medical and health sciencesBacterial ProteinsIn vivoDrug Resistance Multiple BacterialpseudopalinemedicineInner membraneSecretionMolecular Biology030304 developmental biology0303 health sciencesMexAB–OprMBacteriametallophoreChemistry030306 microbiologyPseudomonas aeruginosaMembrane Transport Proteinsbiology.organism_classificationIn vitroCell biology[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyCytoplasmPseudomonas aeruginosaefflux pumpEffluxCell envelopeBacterial outer membraneOligopeptidesBacteriaBacterial Outer Membrane Proteins
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Cadmium and mitochondria

2009

The heavy metal cadmium (Cd) a pollutant associated with several modern industrial processes, is absorbed in significant quantities from cigarette smoke, water, food and air contaminations. It is known to have numerous undesirable effects on health in both experimental animals and humans, targeting kidney, liver and vascular system. The molecular mechanism accounting for most of the biological effects of Cd are not well-understood and the toxicity targets are largely unidentified. The present review focuses on important recent advances about the effects of cadmium on mitochondria of mammalian cells. Mitochondria are the proverbial powerhouses of the cell, running the fundamental biochemical…

Cellchemistry.chemical_elementMitochondrionBiologyModels BiologicalmedicineAnimalsHumansSettore BIO/06 - Anatomia Comparata E CitologiaCytotoxicityMolecular BiologyMembrane potentialMammalsPollutantCadmiumMitochondrial gene expressionApoptosiROSCell BiologyMitochondriamedicine.anatomical_structurechemistryBiochemistryApoptosisToxicityMolecular MedicineEnergy MetabolismIntracellularInner membrane ion permeabilityCadmiumMitochondrion
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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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Subcellular localization of pentachlorophenol 4-monooxygenase in Sphingobium chlorophenolicum ATCC 39723.

2002

Abstract We have studied the subcellular localization of pentachlorophenol 4-monooxygenase (PCP4MO) in Sphingobium chlorophenolicum ATCC 39723 during induction by pentachlorophenol (PCP). Using a monoclonal antibody CL6 specific to the native and recombinant PCP4MO, the enzyme was primarily found soluble as determined by immunoblot and ELISA analyses of cellular fractions. However, the enzyme was observed both in the soluble and membrane-bound forms during induction for 2–4 h, suggesting its translocation out from the cytoplasm. Electron microscopy confirmed that PCP4MO was predominantly present in the cytoplasm at 1 h, whereas at 4 h significant amount was detected also in the membrane and…

CytoplasmBiophysicsBiologyProtein Sorting SignalsBiochemistryMixed Function Oxygenaseschemistry.chemical_compoundBiosynthesisAntibody SpecificityInner membraneMolecular BiologySphingobium chlorophenolicumAlphaproteobacteriachemistry.chemical_classificationAntibodies MonoclonalCell BiologyPeriplasmic spacebiology.organism_classificationSubcellular localizationMolecular biologyImmunohistochemistryPentachlorophenolKineticsEnzymechemistryBiochemistryCytoplasmPeriplasmBiochemical and biophysical research communications
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Phospholipid distribution in the cytoplasmic membrane of Gram-negative bacteria is highly asymmetric, dynamic, and cell shape-dependent

2020

The cell shape of Gram-negative bacteria is maintained metabolically by asymmetric lipid distribution in biogenic plasma membrane.

Gram-negative bacteriaPhospholipidBiochemistryMicrobiology03 medical and health scienceschemistry.chemical_compoundGram-Negative BacteriaCardiolipinEscherichia coliInner membraneCell ShapePhospholipidsResearch Articles030304 developmental biologyPhosphatidylethanolamine0303 health sciencesMultidisciplinarybiologyBilayer030302 biochemistry & molecular biologyCell MembraneSciAdv r-articlesPeriplasmic spacebiology.organism_classificationchemistryCytoplasmBiophysicslipids (amino acids peptides and proteins)Research Article
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PspA adopts an ESCRT-III-like fold and remodels bacterial membranes

2020

SummaryPspA is the main effector of the phage shock protein (Psp) system and preserves the bacterial inner membrane integrity and function. Here, we present the 3.6 Å resolution cryo-EM structure of PspA assembled in helical rods. PspA monomers adopt a canonical ESCRT-III fold in an extended open conformation. PspA rods are capable of enclosing lipids and generate positive membrane curvature. Using cryo-EM we visualized how PspA remodels membrane vesicles into μm-sized structures and how it mediates the formation of internalized vesicular structures. Hot spots of these activities are zones derived from PspA assemblies, serving as lipid transfer platforms and linking previously separated lip…

MembraneMembrane curvatureEffectorChemistryBiophysicsLipid bilayer fusionPhage shockESCRTFunction (biology)Bacterial inner membrane
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