Search results for "Transmembrane"

showing 10 items of 299 documents

Physiology of Zymomonas mobilis: Some Unanswered Questions

2006

The ethanol-producing bacterium Zymomonas mobilis can serve as a model organism for the study of rapid catabolism and inefficient energy conversion in bacteria. Some basic aspects of its physiology still remain poorly understood. Here, the energy-spilling pathways during uncoupled growth, the structure and function of electron transport chain, and the possible reasons for the inefficient oxidative phosphorylation are analysed. Also, the interaction between ethanol synthesis and respiration is considered. The search for mechanisms of futile transmembrane proton cycling, as well as identification of respiratory electron transport complexes, like the energy-coupling NAD(P)H:quinone oxidoreduct…

BiochemistrybiologyCatabolismPhysiologyOxidative phosphorylationNAD+ kinaseQuinone oxidoreductasebiology.organism_classificationNAD(P)H Dehydrogenase (Quinone)Zymomonas mobilisElectron transport chainTransmembrane protein
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Hydrophobic mismatch of mobile transmembrane helices: Merging theory and experiments

2012

Abstract Hydrophobic mismatch still represents a puzzle for transmembrane peptides, despite the apparent simplicity of this concept and its demonstrated validity in natural membranes. Using a wealth of available experimental 2 H NMR data, we provide here a comprehensive explanation of the orientation and dynamics of model peptides in lipid bilayers, which shows how they can adapt to membranes of different thickness. The orientational adjustment of transmembrane α-helices can be understood as the result of a competition between the thermodynamically unfavorable lipid repacking associated with peptide tilting and the optimization of peptide/membrane hydrophobic coupling. In the positive misma…

BiophysicsAnchoringPeptideBiochemistryProtein Structure SecondaryHydrophobic mismatchXWALP peptide familyDynamics of transmembrane peptidesOrientation of transmembrane peptidesWALP peptide familyLipid bilayerPeptide sequencechemistry.chemical_classificationCell MembraneMembrane ProteinsCell BiologyTransmembrane proteinCrystallographyTransmembrane domainMembranechemistryModels ChemicalBiophysicsHydrophobic and Hydrophilic InteractionsPeptide tilt angleSolid-state 2H NMRBiochimica et Biophysica Acta (BBA) - Biomembranes
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Exosome-associated polysialic acid modulates membrane potentials, membrane thermotropic properties, and raft-dependent interactions between vesicles.

2020

In mammals, polysialic acid (polySia) attached to a small number of transmembrane protein carriers occurs on the surface of plasma membranes of neural, cancer, immune, and placental trophoblast cells. Here, our goal was to demonstrate the presence of polySia on exosomes and its effect on membrane properties. We isolated exosomes and found that polysialylated exosomes in fetal bovine serum originate mostly from placental trophoblasts, while in calf bovine serum, they originate from immune cells. Enzymatic removal of polySia chains from the exosomal surface makes the membrane surface potential more positive, transmembrane potential more negative, and reduces the activation energy for membrane…

BiophysicsExosomesBiochemistryExosomeMembrane Potentials03 medical and health sciencesMembrane MicrodomainsStructural BiologyCell Line TumorGeneticsFluorescence Resonance Energy TransferHumansMolecular Biology030304 developmental biologyMembrane potential0303 health sciencesPolysialic acidChemistryVesicle030302 biochemistry & molecular biologyTemperatureCell BiologyMicrovesiclesTransmembrane proteinCell biologyMembraneSialic AcidsAnisotropyanisotropy; exosomes; FRET; membrane potentials; polysialicacid; raftsFetal bovine serumFEBS lettersReferences
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Membrane topology of gp41 and amyloid precursor protein: Interfering transmembrane interactions as potential targets for HIV and Alzheimer treatment

2009

AbstractThe amyloid precursor protein (APP), that plays a critical role in the development of senile plaques in Alzheimer disease (AD), and the gp41 envelope protein of the human immunodeficiency virus (HIV), the causative agent of the acquired immunodeficiency syndrome (AIDS), are single-spanning type-1 transmembrane (TM) glycoproteins with the ability to form homo-oligomers. In this review we describe similarities, both in structural terms and sequence determinants of their TM and juxtamembrane regions. The TM domains are essential not only for anchoring the proteins in membranes but also have functional roles. Both TM segments contain GxxxG motifs that drive TM associations within the li…

BiophysicsHIV InfectionsBiologyGp41BiochemistryArticleTransmembrane segmentAmyloid beta-Protein PrecursorMembranes (Biologia)Alzheimer DiseaseAmyloid precursor proteinAnimalsHumansSenile plaqueschemistry.chemical_classificationCell MembraneMembraneHIVCell Biologygp41HIV Envelope Protein gp41Transmembrane proteinVirusCell biologyTransmembrane domainchemistryBiochemistryAmyloid precursor proteinMembrane topologyAlzheimerHIV-1biology.proteinGlycoproteinSequence motifBiochimica et Biophysica Acta (BBA) - Biomembranes
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Stitching proteins into membranes, not sew simple

2014

Abstract Most integral membrane proteins located within the endomembrane system of eukaryotic cells are first assembled co-translationally into the endoplasmic reticulum (ER) before being sorted and trafficked to other organelles. The assembly of membrane proteins is mediated by the ER translocon, which allows passage of lumenal domains through and lateral integration of transmembrane (TM) domains into the ER membrane. It may be convenient to imagine multi-TM domain containing membrane proteins being assembled by inserting their first TM domain in the correct orientation, with subsequent TM domains inserting with alternating orientations. However a simple threading model of assembly, with s…

BioquímicaChemistryEndoplasmic reticulumClinical BiochemistryProteïnes de membranaMembrane ProteinsNanotechnologyIntracellular MembranesEndoplasmic ReticulumTransloconBiochemistryTransmembrane proteinProtein Structure TertiaryProtein TransportMembraneMembrane proteinBiophysicsAnimalsHumansEndomembrane systemThreading (protein sequence)Molecular BiologyIntegral membrane proteinBiological Chemistry
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Insertion and Topology of a Plant Viral Movement Protein in the Endoplasmic Reticulum Membrane

2002

Virus-encoded movement proteins (MPs) mediate cell-to-cell spread of viral RNA through plant membranous intercellular connections, the plasmodesmata. The molecular pathway by which MPs interact with viral genomes and target plasmodesmata channels is largely unknown. The 9-kDa MP from carnation mottle carmovirus (CarMV) contains two potential transmembrane domains. To explore the possibility that this protein is in fact an intrinsic membrane protein, we have investigated its insertion into the endoplasmic reticulum membrane. By using in vitro translation in the presence of dog pancreas microsomes, we demonstrate that CarMV p9 inserts into the endoplasmic reticulum without the aid of any addi…

BioquímicaGlycosylationMolecular Sequence DataPlasmodesmaBiologyEndoplasmic ReticulumTopologyBiochemistryProtein Structure SecondaryViral ProteinsAmino Acid SequenceMolecular BiologyEndoplasmic reticulumCarmovirusProteïnes de membranaMembrane ProteinsSTIM1Translation (biology)Cell Biologybiology.organism_classificationVirusCell biologyPlant Viral Movement ProteinsTobacco Mosaic VirusTransmembrane domainCytoplasmMembrane topologyCarmovirusJournal of Biological Chemistry
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Double-spanning Plant Viral Movement Protein Integration into the Endoplasmic Reticulum Membrane Is Signal Recognition Particle-dependent, Translocon…

2005

The current model for cell-to-cell movement of plant viruses holds that transport requires virus-encoded movement proteins that intimately associate with endoplasmic reticulum membranes. We have examined the early stages of the integration into endoplasmic reticulum membranes of a double-spanning viral movement protein using photocross-linking. We have discovered that this process is cotranslational and proceeds in a signal recognition particle-dependent manner. In addition, nascent chain photocross-linking to Sec61alpha and translocating chain-associated membrane protein reveal that viral membrane protein insertion takes place via the translocon, as with most eukaryotic membrane proteins, …

BioquímicaSec61Vesicle-associated membrane protein 8Receptors PeptideLipid BilayersReceptors Cytoplasmic and NuclearBiologyEndoplasmic ReticulumBiochemistryViral ProteinsMembranes (Biologia)Escherichia coliMolecular BiologySignal recognition particle receptorSignal recognition particleMembrane GlycoproteinsEndoplasmic reticulumCalcium-Binding ProteinsMembrane ProteinsSTIM1Cell BiologyTransloconTransmembrane proteinCell biologyPlant Viral Movement ProteinsCross-Linking ReagentsMutagenesisRNA ViralCarmovirusSignal Recognition ParticleSEC Translocation Channels
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The CFTR associated protein CAP70 interacts with the apical Cl-/HCO3- exchanger DRA in rabbit small intestinal mucosa.

2005

DRA (down regulated in adenoma) is an intestinal anion exchanger, acting in parallel with NHE3 to facilitate ileal and colonic NaCl absorption. Furthermore it is involved in small intestinal bicarbonate secretion. Because DRA has a PDZ interaction motif, which may influence its properties, we searched for DRA-interacting PDZ adapter proteins in the small intestine. Using an overlay assay with the recombinant DRA C-terminus as a ligand, a 70 kDa protein was labeled, which was restricted to the brush border membrane in rabbit duodenal and ileal mucosa and was not detected in the colon. Destruction of the C-terminal PDZ interaction motif abolished this band, suggesting a specific protein-prote…

Brush borderColonPDZ domainAmino Acid MotifsMolecular Sequence DataCystic Fibrosis Transmembrane Conductance RegulatorIleumBiologyBiochemistryAntiportersCell LineIntestine SmallmedicineAnimalsHumansSecretionAmino Acid SequenceChloride-Bicarbonate AntiportersRNA MessengerIntestinal MucosaMessenger RNAHEK 293 cellsSignal transducing adaptor proteinMembrane ProteinsMolecular biologySmall intestinePeptide Fragmentsmedicine.anatomical_structureSulfate TransportersRabbitsCarrier ProteinsBiochemistry
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Oro-gustatory perception of dietary lipids and calcium signaling in taste bud cells are altered in nutritionally obesity-prone Psammomys obesus.

2013

Since the increasing prevalence of obesity is one of the major health problems of the modern era, understanding the mechanisms of oro-gustatory detection of dietary fat is critical for the prevention and treatment of obesity. We have conducted the present study on Psammomys obesus, the rodent desert gerbil which is a unique polygenic natural animal model of obesity. Our results show that obese animals exhibit a strong preference for lipid solutions in a two-bottle test. Interestingly, the expression of CD36, a lipido-receptor, in taste buds cells (TBC), isolated from circumvallate papillae, was decreased at mRNA level, but remained unaltered at protein level, in obese animals. We further st…

CD36 AntigensMaleTasteAnatomy and PhysiologyCD36BiochemistryCalcium in biologyFatschemistry.chemical_compoundMolecular Cell BiologySignaling in Cellular ProcessesMembrane Receptor Signalingchemistry.chemical_classificationMultidisciplinarybiologyQRTaste PerceptionTaste BudsLipidsSensory SystemsLipid SignalingCytochemistryThapsigarginMedicinePsammomysDisease SusceptibilityIntracellularResearch ArticleSignal Transductionmedicine.medical_specialtyThapsigarginClinical Research DesignLinoleic acidScienceLinoleic AcidFood PreferencesInternal medicinemedicineAnimalsCalcium SignalingObesityAnimal Models of DiseaseBiologyNutritionCell MembraneFatty acidProteinsbiology.organism_classificationLipid MetabolismDietary FatsGustatory SystemTransmembrane ProteinsEndocrinologyMetabolismchemistryGene Expression Regulationbiology.proteinGerbillinaeMembrane CompositionNeurosciencePLoS ONE
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The Role of Cadherins in Ca2+-Mediated Cell Adhesion and Inherited Photoreceptor Degeneration

2002

Cadherins are Ca2+-binding, transmembrane proteins involved in cell adhesion. Recently, three cadherin molecules, cadherin-23, protocadherin-15, and cadherin-3, were found to be defective in various human diseases, many of them with photoreceptor degeneration and/or sensorineural hearing loss as major features such Usher syndrome type 1D (USH1D), USH1F, and hypotrichosis with juvenile macular dystrophy. The process, by which mutations lead to photoreceptor degeneration is still not fully understood. Data from the inner ear phenotype of USH1 mouse models suggest that loss of cell adhesion is a crucial event.

CadherinUsher syndromeMacular dystrophyBiologymedicine.diseasePhenotypeTransmembrane proteinCell biologyRetinitis pigmentosaotorhinolaryngologic diseasesmedicineHypotrichosissense organsCell adhesion
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