Search results for "acids"

showing 10 items of 3520 documents

The production of 85 kDa N-terminal fragment of apolipoprotein B in mutant HepG2 cells generated by targeted modification of apoB gene occurs by ALLN…

2010

Abstract To study the mechanism of low levels of full length and truncated apoB in individuals heterozygous for apoB truncation, a non-sense mutation was introduced in one of the three alleles of apob gene of HepG2 cells by homologous recombination. Despite very low levels of apoB-82 (1–2%) in the media, a prominent N-terminal apoB protein of 85 kDa (apoB-15) was secreted that fractionated at d > 1.065 in density gradient ultracentrifugation. The mechanism of production of this short protein was studied by 35S-methionine pulse–chase experiment. Oleate prevented presecretory degradation of apoB-100 in the cell and resulted in increased secretion of newly synthesized apoB-100 with decreases i…

Protein FoldingHepG2Apolipoprotein BLeupeptinsmedicine.medical_treatmentMutantBiophysicsBiologyCysteine Proteinase Inhibitorsdigestive systemBiochemistry85 kDa N-terminalCysteine ProteasesapoBmedicineHumansSecretionMolecular BiologyApolipoproteins BProteasenutritional and metabolic diseasesCell BiologyHep G2 CellsCysteine proteaseMolecular biologyTransmembrane proteinProtein TransportCodon NonsenseHypobetalipoproteinemia Familial Apolipoprotein Bbiology.proteinlipids (amino acids peptides and proteins)Density gradient ultracentrifugationIntracellular
researchProduct

The membrane environment modulates self-association of the human GpA TM domain--implications for membrane protein folding and transmembrane signaling.

2010

Abstract The influence of lipid bilayer properties on a defined and sequence-specific transmembrane helix–helix interaction is not well characterized yet. To study the potential impact of changing bilayer properties on a sequence-specific transmembrane helix–helix interaction, we have traced the association of fluorescent-labeled glycophorin A transmembrane peptides by fluorescence spectroscopy in model membranes with varying lipid compositions. The observed changes of the glycophorin A dimerization propensities in different lipid bilayers suggest that the lipid bilayer thickness severely influences the monomer–dimer equilibrium of this transmembrane domain, and dimerization was most effici…

Protein FoldingLipid BilayersMolecular Sequence DataBiophysicsGpABiochemistryFluorescenceMembrane LipidsOrientations of Proteins in Membranes databaseMembrane fluidityFluorescence Resonance Energy TransferHumansAmino Acid SequenceGlycophorinsBilayerLipid bilayerIntegral membrane proteinBinding SitesChemistryBilayerPeripheral membrane proteinTemperatureMembrane ProteinsCell BiologyTransmembrane proteinCell biologyTransmembrane domainCholesterolSpectrometry FluorescenceFRETPhosphatidylcholineslipids (amino acids peptides and proteins)Transmembrane helix–helix interactionProtein MultimerizationPeptidesHydrophobic and Hydrophilic InteractionsSignal TransductionBiochimica et biophysica acta
researchProduct

Polar/Ionizable Residues in Transmembrane Segments: Effects on Helix-Helix Packing

2012

The vast majority of membrane proteins are anchored to biological membranes through hydrophobic alpha-helices. Sequence analysis of high-resolution membrane protein structures show that ionizable amino acid residues are present in transmembrane (TM) helices, often with a functional and/or structural role. Here, using as scaffold the hydrophobic TM domain of the model membrane protein glycophorin A (GpA), we address the consequences of replacing specific residues by ionizable amino acids on TM helix insertion and packing, both in detergent micelles and in biological membranes. Our findings demonstrate that ionizable residues are stably inserted in hydrophobic environments, and tolerated in t…

Protein Foldinglcsh:MedicineBiochemistryBiotecnologiaProtein Structure SecondaryCell membraneGlycophorinsAmino Acidslcsh:ScienceMicelleschemistry.chemical_classificationMultidisciplinarybiologySodium Dodecyl SulfateLipidsTransmembrane proteinAmino acidmedicine.anatomical_structureBiochemistryCytochemistryThermodynamicsResearch ArticleProtein StructureBiophysicsCalcium-Transporting ATPasesProtein ChemistryProtein–protein interactionMembranes (Biologia)MicrosomesEscherichia colimedicineGlycophorinProtein InteractionsBiologyCell Membranelcsh:RMembrane ProteinsProteinsComputational BiologyBiological membraneIntracellular MembranesProtein Structure TertiaryTransmembrane ProteinsMembrane proteinchemistryHelixbiology.proteinBiophysicslcsh:QProtein Multimerization
researchProduct

Dual film-like organelles enable spatial separation of orthogonal eukaryotic translation

2021

Summary Engineering new functionality into living eukaryotic systems by enzyme evolution or de novo protein design is a formidable challenge. Cells do not rely exclusively on DNA-based evolution to generate new functionality but often utilize membrane encapsulation or formation of membraneless organelles to separate distinct molecular processes that execute complex operations. Applying this principle and the concept of two-dimensional phase separation, we develop film-like synthetic organelles that support protein translation on the surfaces of various cellular membranes. These sub-resolution synthetic films provide a path to make functionally distinct enzymes within the same cell. We use t…

Protein designComputational biologyBiology2D phase separationArticleGeneral Biochemistry Genetics and Molecular BiologySynthetic biologyEukaryotic translationOrganelleHumansRNA MessengerAmino AcidsOrganellesmembrane signalingsynthetic biomolecular condensatesProteinsTranslation (biology)Intracellular MembranesProtein engineeringGenetic codeenzyme engineeringHEK293 Cellsgenetic code expansionEukaryotic CellsGenetic CodeProtein Biosynthesisorthogonal translationsynthetic biologyRibosomesFunction (biology)Cell
researchProduct

Perturbed interactions of mutant proteolipid protein/DM20 with cholesterol and lipid rafts in oligodendroglia: implications for dysmyelination in spa…

2006

Missense mutations in the humanPLP1gene lead to dysmyelinating diseases with a broad range of clinical severity, ranging from severe Pelizaeus–Merzbacher disease (PMD) to milder spastic paraplegia type 2 (SPG-2). The molecular pathology has been generally attributed to endoplasmic reticulum (ER) retention of misfolded proteolipid protein (PLP) (and its splice isoform DM20) and induction of the unfolded protein response. As opposed to previous studies of heterologous expression systems, we have analyzed PLP/DM20 trafficking in oligodendroglial cells, thereby revealing differences between PMD and SPG-2-associated PLP/DM20 isoforms. PLPA242Vand DM20A242V(jimpy-msdin mice), associated with seve…

Proteolipid protein 1Time FactorsLeupeptinsBlotting WesternGene Expressionchemical and pharmacologic phenomenaNerve Tissue ProteinsBiologyProtein degradationCysteine Proteinase InhibitorsTransfectionMiceMice Neurologic MutantsCricetulusMembrane MicrodomainsMutant proteinimmune system diseasesCricetinaeAnimalsImmunoprecipitationMyelin Proteolipid ProteinLipid raftCells CulturedGeneral NeuroscienceEndoplasmic reticulumCholesterol bindingER retentionArticlesImmunohistochemistryCell biologynervous system diseasesOligodendrogliaProtein TransportCholesterolBiochemistryUnfolded protein responselipids (amino acids peptides and proteins)Mutant ProteinsSubcellular FractionsThe Journal of neuroscience : the official journal of the Society for Neuroscience
researchProduct

Differential proteomic analysis highlights metabolic strategies associated with balhimycin production in Amycolatopsis balhimycina chemostat cultivat…

2010

Abstract Background Proteomics was recently used to reveal enzymes whose expression is associated with the production of the glycopeptide antibiotic balhimycin in Amycolatopsis balhimycina batch cultivations. Combining chemostat fermentation technology, where cells proliferate with constant parameters in a highly reproducible steady-state, and differential proteomics, the relationships between physiological status and metabolic pathways during antibiotic producing and non-producing conditions could be highlighted. Results Two minimal defined media, one with low Pi (0.6 mM; LP) and proficient glucose (12 g/l) concentrations and the other one with high Pi (1.8 mM) and limiting (6 g/l; LG) glu…

Proteomemedicine.drug_classlcsh:QR1-502BioengineeringChemostatBiologyGlycopeptide antibioticProteomicsSettore BIO/19 - Microbiologia GeneraleApplied Microbiology and Biotechnologylcsh:Microbiology03 medical and health sciencesBacterial ProteinsVancomycinantibioticActinomycetalesmedicineElectrophoresis Gel Two-DimensionalBalhimycinproteomic030304 developmental biology2. Zero hungerchemistry.chemical_classification0303 health sciences030306 microbiologyResearchFatty AcidsCarbonAnti-Bacterial AgentsMetabolic pathwayglycopeptideEnzymeGlucosechemistryBiochemistryAmycolatopsis balhimycinaProtein BiosynthesisFermentationBiotechnologyMicrobial Cell Factories
researchProduct

Fumarate dependent protein composition under aerobic and anaerobic growth conditions in Escherichia coli

2020

Abstract In the absence of sugars, C4-dicarboxylates (C4DC) like fumarate represent important substrates for growth of Escherichia coli. Aerobically, C4DCs are oxidized to CO2 whereas anaerobically, C4DCs are used for fumarate respiration. In order to determine the impact of fumarate under aerobic and anaerobic conditions, proteomes of E. coli W3110 grown aerobically or anaerobically with fumarate and/or the non-C4DC substrate glycerol were comparatively profiled by nanoLC-MS/MS. Membrane enrichment allowed sensitive detection of membrane proteins. A total of 1657 proteins of which 646 and 374 were assigned to the cytosol or membrane, respectively, were covered. Presence of fumarate trigger…

Proteomics0301 basic medicineBiophysicsCatabolite repressionmedicine.disease_causeBiochemistryCarbon utilization03 medical and health sciencesFumaratesTandem Mass SpectrometryEscherichia colimedicineDicarboxylic AcidsAnaerobiosisEscherichia coli030102 biochemistry & molecular biologybiologyChemistryEscherichia coli ProteinsGene Expression Regulation BacterialAerobiosisDNA-Binding ProteinsCitric acid cycle030104 developmental biologyRegulonMembrane proteinBiochemistrycAMP receptor proteinbiology.proteinProtein KinasesAnaerobic exerciseTranscription FactorsJournal of Proteomics
researchProduct

TrpM, a Small Protein Modulating Tryptophan Biosynthesis and Morpho-Physiological Differentiation in Streptomyces coelicolor A3(2).

2016

In the model actinomycete Streptomyces coelicolor A3(2), small open reading frames encoding proteins with unknown functions were identified in several amino acid biosynthetic gene operons, such as SCO2038 (trpX) in the tryptophan trpCXBA locus. In this study, the role of the corresponding protein in tryptophan biosynthesis was investigated by combining phenotypic and molecular analyses. The 2038KO mutant strain was characterized by delayed growth, smaller aerial hyphae and reduced production of spores and actinorhodin antibiotic, with respect to the WT strain. The capability of this mutant to grow on minimal medium was rescued by tryptophan and tryptophan precursor (serine and/or indole) su…

Proteomics0301 basic medicineProtein ExtractionMutantlcsh:MedicineStreptomyces coelicolor A3(2)Settore BIO/19 - Microbiologia GeneraleBiochemistrySerinechemistry.chemical_compoundAromatic Amino AcidsSmall ProteinAntibioticsTRPMMicrobial PhysiologyMedicine and Health SciencesBacterial PhysiologyAmino Acidslcsh:ScienceProtein MetabolismExtraction TechniquesMultidisciplinarybiologyOrganic CompoundsAntimicrobialsStreptomyces coelicolorTryptophanDrugsChemistryBiochemistryPhysical SciencesPhysiological DifferentiationResearch ArticleTryptophan BiosynthesiSmall Protein; Biosynthesis; Morpho-Physiological Differentiation: Streptomyces coelicolorBiosynthesisResearch and Analysis MethodsMicrobiologyStreptomycesActinorhodin03 medical and health sciencesBiosynthesisMicrobial ControlBacterial SporesPharmacology030102 biochemistry & molecular biologyOrganic Chemistrylcsh:RChemical CompoundsTryptophanTrpM; Small Protein; Tryptophan Biosynthesis; Morphological Differentiation; Physiological Differentiation; Streptomyces coelicolor A3(2); ProteomicsBiology and Life SciencesProteinsBacteriologybiology.organism_classificationAmino Acid MetabolismMetabolism030104 developmental biologychemistrylcsh:QMorphological DifferentiationTrpM
researchProduct

Stuck at work? Quantitative proteomics of environmental wine yeast strains reveals the natural mechanism of overcoming stuck fermentation

2015

During fermentation oenological yeast cells are subjected to a number of different stress conditions and must respond rapidly to the continuously changing environment of this harsh ecological niche. In this study we gained more insights into the cell adaptation mechanisms by linking proteome monitoring with knowledge on physiological behaviour of different strains during fermentation under model winemaking conditions. We used 2D-DIGE technology to monitor the proteome evolution of two newly discovered environmental yeast strains Saccharomyces bayanus and triple hybrid Saccharomyces cerevisiae × Saccharomyces kudriavzevii × S. bayanus and compared them to data obtained for the commercially a…

Proteomics0301 basic medicineProteomeSaccharomyces cerevisiaeSaccharomyces bayanusWineSaccharomyces cerevisiaeBiologyBiochemistrySaccharomycesFungal ProteinsTwo-Dimensional Difference Gel ElectrophoresisSaccharomyces03 medical and health sciencesStress PhysiologicalAmino AcidsMolecular BiologyEthanolCell redox homeostasisbiology.organism_classificationYeastStuck fermentationBiosynthetic PathwaysProtein TransportYeast in winemaking030104 developmental biologyBiochemistryFermentationProteolysisGlycolysisOxidation-ReductionSaccharomyces kudriavzeviiPROTEOMICS
researchProduct

The Metalloprotease Meprin β Generates Amino Terminal-truncated Amyloid β Peptide Species

2012

The amyloid β (Aβ) peptide, which is abundantly found in the brains of patients suffering from Alzheimer disease, is central in the pathogenesis of this disease. Therefore, to understand the processing of the amyloid precursor protein (APP) is of critical importance. Recently, we demonstrated that the metalloprotease meprin β cleaves APP and liberates soluble N-terminal APP (N-APP) fragments. In this work, we present evidence that meprin β can also process APP in a manner reminiscent of β-secretase. We identified cleavage sites of meprin β in the amyloid β sequence of the wild type and Swedish mutant of APP at positions p1 and p2, thereby generating Aβ variants starting at the first or seco…

ProteomicsMolecular Sequence DataMutantPeptideBiologyHydroxamic AcidsCleavage (embryo)BiochemistryCatalysis03 medical and health sciences0302 clinical medicineAlzheimer Diseasemental disordersmedicineAmyloid precursor proteinHumansProtein IsoformsAmino Acid SequenceMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMetalloproteinaseAmyloid beta-PeptidesWild typeBrainMetalloendopeptidasesMolecular Bases of DiseaseCell Biologymedicine.diseaseMolecular biologyProtein Structure TertiaryKineticsHEK293 CellsEnzymechemistryBiochemistryMutationMetalloproteasesbiology.proteinAmyloid Precursor Protein SecretasesAlzheimer's diseasePeptides030217 neurology & neurosurgeryJournal of Biological Chemistry
researchProduct