Search results for "Membrane Proteins"

showing 10 items of 713 documents

Cloning and characterization of CSP37, a novel gene encoding a putative membrane protein of Candida albicans.

1997

In the course of an analysis of the functions and assembly of the cell wall of Candida albicans, we have cloned and characterized a gene, which we designated CSP37 (cell surface protein), encoding a 37-kDa polypeptide which is a membrane-associated protein. The gene was isolated by immunological screening of a DNA library constructed from mycelial cells with a polyclonal serum raised against cell walls of this morphology. Analysis of the nucleotide sequence of a corresponding genomic DNA fragment revealed a single open reading frame which encodes a predicted protein of 321 amino acids with no significant homology to others in the databases. Disruption of the CSP37 gene by the method describ…

Vesicle-associated membrane protein 8HeterozygoteRecombinant Fusion ProteinsMutantGenes FungalMolecular Sequence DataBiologyMicrobiologyRetinoblastoma-like protein 1Fungal ProteinsMiceHSPA2SNAP23Candida albicansEscherichia coliAnimalsAmino Acid SequenceCloning MolecularDNA FungalMolecular BiologyGeneHSPA9Mice Inbred BALB CBase SequenceHomozygoteMembrane ProteinsSequence Analysis DNABlotting NorthernMolecular biologyPhenotypeAKT1S1Gene DeletionResearch ArticleJournal of bacteriology
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Tissue expression of the vesicle protein pantophysin

1999

The cell-type restricted expression of cytoplasmic microvesicle membrane protein isoforms may be a consequence of the functional adaptation of these vesicles to the execution of specialized processes in cells of different specialization. To characterize the expression of the vesicle protein pantophysin, an isoform of the synaptic vesicle proteins synaptophysin and synaptoporin, we have prepared and characterized antibodies useful for the immunological detection of pantophysin in vitro and in situ. Using these reagents, we show by immunoblot analyses that pantophysin expression is not homogeneous but differs significantly between various bovine tissues. Furthermore, these differences are not…

Vesicle-associated membrane protein 8Membrane GlycoproteinsHistologySynaptobrevinMicrovesicleMembrane ProteinsSNAP25Cell BiologySynaptoporinBiologyCytoplasmic GranulesMolecular biologyPathology and Forensic MedicineCell biologyR-SNARE ProteinsVesicle-associated membrane proteinMembrane proteinOrgan SpecificitySynaptophysinbiology.proteinAnimalsProtein IsoformsCattleCarrier ProteinsFluorescent Antibody Technique IndirectCell and Tissue Research
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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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Membrane topology and post-translational modification of the Saccharomyces cerevisiae essential protein Rot1.

2007

ROT1 is an essential gene that has been related to cell wall biosynthesis, the actin cytoskeleton and protein folding. In order to help to understand its molecular function, we carried out a characterization of the Rot1 protein. It is primarily located at the endoplasmic reticulum-nuclear membrane facing the lumen. Rot1 migrates more slowly than expected, which might suggest post-translational modification. Our results indicate that Rot1 is a protein that is neither GPI-anchored nor O-glycosylated. In contrast, it is N-glycosylated. By a directed mutagenesis of several Asn residues, we identified that the protein is simultaneously glycosylated at N103, N107 and N139. Although the mutation o…

Vesicle-associated membrane protein 8Saccharomyces cerevisiae ProteinsMolecular Sequence DataBioengineeringmacromolecular substancesSaccharomyces cerevisiaeBiologyEndoplasmic ReticulumApplied Microbiology and BiotechnologyBiochemistryProtein structureSEC62Gene Expression Regulation FungalGeneticsAmino Acid SequenceCell MembraneMembrane ProteinsActin cytoskeletonCell biologyTransport proteinProtein Structure TertiaryTransmembrane domainProtein TransportBiochemistryMembrane topologyProtein foldingProtein Processing Post-TranslationalBiotechnologyMolecular ChaperonesYeast (Chichester, England)
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Purified Membrane-Containing Procapsids of Bacteriophage PRD1 Package the Viral Genome

2009

Icosahedral-tailed double-stranded DNA (dsDNA) bacteriophages and herpesviruses translocate viral DNA into a preformed procapsid in an ATP-driven reaction by a packaging complex that operates at a portal vertex. A similar packaging system operates in the tailless dsDNA phage PRD1 (Tectiviridae family), except that there is an internal membrane vesicle in the procapsid. The unit-length linear dsDNA genome with covalently linked 5'-terminal proteins enters the procapsid through a unique vertex. Two small integral membrane proteins, P20 and P22, provide a conduit for DNA translocation. The packaging machinery also contains the packaging ATPase P9 and the packaging efficiency factor P6. Here we…

Viral Plaque AssayvirusesATPaseViral Plaque AssayGenomeViral Proteins03 medical and health scienceschemistry.chemical_compoundCapsidBacteriophage PRD1Structural BiologyBacteriophage PRD1Molecular BiologyIntegral membrane protein030304 developmental biology0303 health sciencesMicrobial Viabilitybiology030306 microbiologyVirus AssemblyCell MembraneMembrane ProteinsMolecular biologyMembranechemistryDNA Viralbiology.proteinBiophysicsTectiviridaeDNAJournal of Molecular Biology
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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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Membrane Insertion and Biogenesis of the Turnip Crinkle Virus p9 Movement Protein

2010

ABSTRACT Plant viral infection and spread depends on the successful introduction of a virus into a cell of a compatible host, followed by replication and cell-to-cell transport. The movement proteins (MPs) p8 and p9 of Turnip crinkle virus are required for cell-to-cell movement of the virus. We have examined the membrane association of p9 and found that it is an integral membrane protein with a defined topology in the endoplasmic reticulum (ER) membrane. Furthermore, we have used a site-specific photo-cross-linking strategy to study the membrane integration of the protein at the initial stages of its biosynthetic process. This process is cotranslational and proceeds through the signal recog…

VirologiavirusesImmunologyEndoplasmic ReticulumMicrobiologyVirusMembranes (Biologia)VirologyMovement proteinIntegral membrane proteinSignal recognition particlebiologyTurnip crinkle virusEndoplasmic reticulumProteïnes de membranaMembrane Proteinsbiology.organism_classificationVirus-Cell InteractionsVirusCell biologyPlant Viral Movement ProteinsMembrane proteinBiochemistryInsect ScienceBiosynthetic processCarmovirusSignal Recognition ParticleJournal of Virology
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Sec61alpha and TRAM are Sequentially Adjacent to a Nascent Viral Membrane Protein during its ER Integration

2007

Co-translational integration of a nascent viral membrane protein into the endoplasmic reticulum membrane takes place via the translocon. We have been studying the early stages of the integration of a double-spanning plant viral movement protein to gain insights into how viral membrane proteins are transferred from the hydrophilic interior of the translocon into the hydrophobic environment of the bilayer, where the transmembrane (TM) segments of the viral proteins can diffuse freely. Photocrosslinking experiments reveal that this integration involves the sequential passage of the TM segments past Sec61alpha and translocating chain-associating membrane protein (TRAM). Each TM segment is first…

Virus IntegrationBiologyEndoplasmic ReticulumModels BiologicalViral Matrix ProteinsDogsMembranes (Biologia)Structural BiologyAnimalsRNA MessengerMolecular BiologyVirus IntegrationMembrane GlycoproteinsViral matrix proteinEndoplasmic reticulumProteïnes de membranaMembrane ProteinsViral membraneTransloconTransmembrane proteinCell biologyPlant Viral Movement ProteinsCross-Linking ReagentsMembrane proteinBiochemistrySEC Translocation ChannelsSEC Translocation ChannelsMolecular Chaperones
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Depletion ofL-arginine induces autophagy as a cytoprotective response to endoplasmic reticulum stress in human T lymphocytes

2012

PMCID: PMC3494587

X-Box Binding Protein 1Proteasome Endopeptidase ComplexProgrammed cell deathXBP1CD3 ComplexMAP Kinase Signaling SystemRNA SplicingT-LymphocytesT cellDown-RegulationApoptosisRegulatory Factor X Transcription FactorsUbiquitin-Activating EnzymesProtein Serine-Threonine KinasesBiologyArginineLymphocyte ActivationAutophagy-Related Protein 7Jurkat cellsJurkat CellsEndoribonucleasesAutophagymedicineHumansMolecular BiologyCell ProliferationTOR Serine-Threonine KinasesAutophagyMembrane ProteinsCell BiologyBECN1Endoplasmic Reticulum StressG1 Phase Cell Cycle CheckpointsBasic Research Paper3. Good healthCell biologyDNA-Binding Proteinsmedicine.anatomical_structureCytoprotectionApoptosisUnfolded protein responseBeclin-1MitogensApoptosis Regulatory ProteinsLysosomesProto-Oncogene Proteins c-aktTranscription FactorsAutophagy
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The membrane proteome of Medicago truncatula roots displays qualitative and quantitative changes in response to arbuscular mycorrhizal symbiosis

2014

International audience; Arbuscular mycorrhizal (AM) symbiosis that associates roots of most land plants with soil-borne fungi (Glomeromycota), is characterized by reciprocal nutritional benefits. Fungal colonization of plant roots induces massive changes in cortical cells where the fungus differentiates an arbuscule, which drives proliferation of the plasma membrane. Despite the recognized importance of membrane proteins in sustaining AM symbiosis, the root microsomal proteome elicited upon mycorrhiza still remains to be explored. In this study, we first examined the qualitative composition of the root membrane proteome of Medicago truncatula after microsome enrichment and subsequent in dep…

[SDV.SA]Life Sciences [q-bio]/Agricultural sciencesGeLC-MS/MS[SDV.BIO]Life Sciences [q-bio]/BiotechnologyProteomeBiophysicsBiological Transport ActiveRoot membrane proteomeBiochemistrySpectral countingFungal ProteinsGlomeromycotaSymbiosisPeriarbuscular membraneMycorrhizaeMedicago truncatulaBotanyEndomembrane systemMycorrhizaArbuscular mycorrhizaRhizophagus irregularisSymbiosisPlant Proteins2. Zero hungerbiologyfungiMembrane Proteins15. Life on landbiology.organism_classificationMedicago truncatulaCell biologyMembrane proteinProteomeSignal Transduction
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