Search results for "carrier protein"

showing 10 items of 361 documents

Functioning of DcuC as the C 4 -Dicarboxylate Carrier during Glucose Fermentation by Escherichia coli

1999

ABSTRACT The dcuC gene of Escherichia coli encodes an alternative C 4 -dicarboxylate carrier (DcuC) with low transport activity. The expression of dcuC was investigated. dcuC was expressed only under anaerobic conditions; nitrate and fumarate caused slight repression and stimulation of expression, respectively. Anaerobic induction depended mainly on the transcriptional regulator FNR. Fumarate stimulation was independent of the fumarate response regulator DcuR. The expression of dcuC was not significantly inhibited by glucose, assigning a role to DcuC during glucose fermentation. The inactivation of dcuC increased fumarate-succinate exchange and fumarate uptake by DcuA and DcuB, suggesting a…

Physiology and MetabolismMolecular Sequence DataMutantStimulationBiologymedicine.disease_causeMicrobiologyBacterial ProteinsFumaratesConsensus SequenceEscherichia colimedicineTranscriptional regulationDicarboxylic AcidsAnaerobiosisPromoter Regions GeneticMolecular BiologyEscherichia coliPsychological repressionDicarboxylic Acid TransportersBinding SitesBase SequenceEscherichia coli ProteinsSuccinatesGene Expression Regulation BacterialKineticsResponse regulatorGlucoseBiochemistryFermentationFermentationEffluxCarrier ProteinsRibosomesJournal of Bacteriology
researchProduct

Identification of the Weevil immune genes and their expression in the bacteriome tissue

2008

Abstract Background Persistent infections with mutualistic intracellular bacteria (endosymbionts) are well represented in insects and are considered to be a driving force in evolution. However, while pathogenic relationships have been well studied over the last decades very little is known about the recognition of the endosymbionts by the host immune system and the mechanism that limits their infection to the bacteria-bearing host tissue (the bacteriome). Results To study bacteriome immune specificity, we first identified immune-relevant genes of the weevil Sitophilus zeamais by using suppressive subtractive hybridization (SSH) and then analyzed their full-length coding sequences obtained b…

PhysiologyPlant Scienceprotéines et peptides de signalisation intracellulaireStructural BiologyGene expressionlcsh:QH301-705.5Genetics0303 health sciencesAgricultural and Biological Sciences(all)EndosymbiosisReverse Transcriptase Polymerase Chain ReactionMicrobiology and ParasitologyIntracellular Signaling Peptides and ProteinsMicrobiologie et ParasitologielarveLarva1-1-1 Article périodique à comité de lectureInsect ProteinsGeneral Agricultural and Biological SciencesResearch ArticleBiotechnologyexpression géniquecharanconMolecular Sequence DatamuramidaseBiologyGeneral Biochemistry Genetics and Molecular BiologyMicrobiology03 medical and health sciencesAposymbioticcurculionidaeImmune systemEscherichia coliAnimalsGeneEcology Evolution Behavior and SystematicsAlphaproteobacteria030304 developmental biologyBiochemistry Genetics and Molecular Biology(all)030306 microbiologyTOLLIPIntracellular parasitefungiBacteriomeCell Biologybiochemical phenomena metabolism and nutritionGene Expression Regulationlcsh:Biology (General)WeevilsbacteriaCarrier ProteinsAntimicrobial Cationic Peptides[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/SymbiosisDevelopmental BiologyBMC Biology
researchProduct

The fungal elicitor cryptogein is a sterol carrier protein

1997

AbstractCryptogein is a protein secreted by the phytopathogenic pseudo-fungus, Phytophthora cryptogea. It is a basic 10 kDa hydrophilic protein having a hydrophobic pocket and three disulfide bridges. These common features with sterol carrier proteins led us to investigate its possible sterol transfer activity using the fluorescent sterol, dehydroergosterol. The results show that cryptogein has one binding site with strong affinity for dehydroergosterol. Moreover, this protein catalyzes the transfer of sterols between phospholipidic artificial membranes. This is the first evidence for the existence of an extracellular sterol carrier protein and for a molecular activity of cryptogein. This p…

Phytophthora0106 biological sciencesBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular Biology01 natural sciencesBiochemistryFluorescenceFungal Proteins03 medical and health scienceschemistry.chemical_compoundStructural BiologyErgosterolPhosphatidylcholinepolycyclic compoundsGeneticsExtracellularBinding siteMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesbiologyPhytophthora cryptogeaAlgal ProteinsElicitinCell Biologybiology.organism_classificationElicitinSterolElicitorKineticsCholesterolSpectrometry FluorescenceSterol carrier proteinDehydroergosterolBiochemistrychemistryLiposomeslipids (amino acids peptides and proteins)Carrier Proteins010606 plant biology & botany
researchProduct

Modulation of the Biological Activity of a Tobacco LTP1 by Lipid Complexation

2004

Plant lipid transfer proteins (LTPs) are small, cysteine-rich proteins secreted into the extracellular space. They belong to the pathogenesis-related proteins (PR-14) family and are believed to be involved in several physiological processes including plant disease resistance, although their precise biological function is still unknown. Here, we show that a recombinant tobacco LTP1 is able to load fatty acids and jasmonic acid. This LTP1 binds to specific plasma membrane sites, previously characterized as elicitin receptors, and is shown to be involved in the activation of plant defense. The biological properties of this LTP1 were compared with those of LTP1-linolenic and LTP1-jasmonic acid…

Phytophthora0106 biological sciences[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringCyclopentanesPlasma protein bindingBiologyFatty Acid-Binding ProteinsLigands01 natural sciencesMass SpectrometryFatty acid-binding proteinCell membrane03 medical and health scienceschemistry.chemical_compoundTobacco[SDV.IDA]Life Sciences [q-bio]/Food engineeringExtracellularmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringOxylipinsMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesDose-Response Relationship DrugCircular DichroismJasmonic acidCell MembraneFatty AcidsElicitinBiological activityArticlesCell Biology[SDV.IDA] Life Sciences [q-bio]/Food engineeringLipid MetabolismLipidsRecombinant Proteinsmedicine.anatomical_structureBiochemistrychemistryPHYTOPHTORA PARASITICACarrier ProteinsTRANSFERT LIPIDIQUEPlant lipid transfer proteinsChromatography LiquidProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
researchProduct

Identification of a plasminogen-binding motif in PAM, a bacterial surface protein.

1995

Surface-associated plasmin(ogen) may contribute to the invasive properties of various cells. Analysis of plasmin(ogen)-binding surface proteins is therefore of interest. The N-terminal variable regions of M-like (ML) proteins from five different group A streptococcal serotypes (33, 41, 52, 53 and 56) exhibiting the plasminogen-binding phenotype were cloned and expressed in Escherichia coli. The recombinant proteins all bound plasminogen with high affinity. The binding involved the kringle domains of plasminogen and was blocked by a lysine analogue, 6-aminohexanoic acid, indicating that lysine residues in the M-like proteins participate in the interaction. Sequence analysis revealed that the…

PlasminStreptococcus pyogenesMolecular Sequence DataPlasma protein bindingBiologyMicrobiologyKringle domainBacterial ProteinsKringlesmedicineEscherichia coliAmino Acid SequenceBinding siteCloning MolecularMolecular BiologyPeptide sequenceBinding SitesBase SequenceLysinePlasminogenFusion proteinMolecular biologyRecombinant ProteinsPhenotypeBiochemistryCarrier ProteinsPlasminogen activatorSequence AlignmentBinding domainmedicine.drugProtein BindingMolecular microbiology
researchProduct

Mutations in MTP gene in abeta- and hypobeta-lipoproteinemia.

2005

Abstract Familial hypobetalipoproteinemia (FHBL) and abetalipoproteinemia (ABL) are inherited disorders of apolipoprotein B (apo B)-containing lipoproteins that result from mutations in apo B and microsomal triglyceride transfer protein (MTP) genes, respectively. Here we report three patients with severe deficiency of plasma low-density lipoprotein (LDL) and apo B. Two of them (probands F.A. and P.E.) had clinical and biochemical phenotype consistent with ABL. Proband F.A. was homozygous for a minute deletion/insertion (c.1228delCCCinsT) in exon 9 of MTP gene predicted to cause a truncated MTP protein of 412 amino acids. Proband P. E. was heterozygous for a mutation in intron 9 (IVS9-1G>A),…

ProbandApolipoprotein EAdultMaleSettore MED/09 - Medicina InternaApolipoprotein BGenotypeDNA Mutational AnalysisGene mutationCompound heterozygosityHypobetalipoproteinemiasApo B genemedicineMissense mutationHumansGene mutationApo E genotypeGeneticsbiologyAbetalipoproteinemia; Hypobetalipoproteinemia; MTP gene; Apo B gene; Gene mutations; Apo E genotypeAbetalipoproteinemiamedicine.diseaseAbetalipoproteinemiaPedigreePhenotypeChild Preschoolbiology.proteinlipids (amino acids peptides and proteins)FemaleHypobetalipoproteinemiaMTP geneCardiology and Cardiovascular MedicineCarrier ProteinsHypobetalipoproteinemia
researchProduct

Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational…

2003

The large L envelope protein of the hepatitis B virus utilizes a new folding pathway to acquire a dual transmembrane topology in the endoplasmic reticulum (ER). The process involves cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain into the ER. Here, we demonstrate that the conformational and functional heterogeneity of L depends on the action of molecular chaperones. Using coimmunoprecipitation, we observed specific interactions between L and the cytosolic Hsc70, in conjunction with Hsp40, and between L and the ER-resident BiP in mammalian cells. Complex formation between L and Hsc70 was abolished when preS translocation was artifici…

Protein ConformationImmunoprecipitationHSC70 Heat-Shock Proteinsmacromolecular substancesTopologyProtein structureViral Envelope ProteinsAnimalsHSP70 Heat-Shock ProteinsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsMultidisciplinarybiologyEndoplasmic reticulumHSC70 Heat-Shock ProteinsBiological SciencesPrecipitin TestsTransport proteinProtein TransportMembrane topologyChaperone (protein)COS Cellsbiology.proteinProtein topologyCarrier ProteinsProtein Processing Post-TranslationalMolecular ChaperonesProceedings of the National Academy of Sciences
researchProduct

Crystallization and preliminary X-ray studies of oligandrin, a sterol-carrier elicitor fromPythium oligandrum

2000

Oligandrin is a 10 kDa acidic protein produced by the fungus micromycete Pythium oligandrum and is a member of the alpha-elicitin group, with sterol- and lipid-carrier properties. Oligandrin has been crystallized at 290 K using PEG 4000 as a precipitant. A cholesterol complex was obtained under the same conditions. The space group of the crystals at low temperature (100 K) is C222, with unit-cell parameters a = 94.0, b = 171.1, c = 55.3 A. Four molecules are present in the asymmetric unit. Data from the free and cholesterol-complexed forms were recorded at synchrotron sources to resolutions of 2.4 (uncomplexed) and 1.9 A (complexed), respectively.

Protein ConformationPythiumElicitinGeneral MedicineBiologyCrystallography X-Raybiology.organism_classificationSterolElicitorlaw.inventionFungal ProteinsSterolsCrystallographyCholesterolSterol carrier proteinStructural BiologylawPEG ratioIntercellular Signaling Peptides and ProteinsMoleculeElectrophoresis Polyacrylamide GelCrystallizationCarrier ProteinsCrystallizationPythium oligandrumActa Crystallographica Section D Biological Crystallography
researchProduct

Investigation of protein folding by coarse-grained molecular dynamics with the UNRES force field.

2010

Coarse-grained molecular dynamics simulations offer a dramatic extension of the time-scale of simulations compared to all-atom approaches. In this article, we describe the use of the physics-based united-residue (UNRES) force field, developed in our laboratory, in protein-structure simulations. We demonstrate that this force field offers about a 4000-times extension of the simulation time scale; this feature arises both from averaging out the fast-moving degrees of freedom and reduction of the cost of energy and force calculations compared to all-atom approaches with explicit solvent. With massively parallel computers, microsecond folding simulation times of proteins containing about 1000 r…

Protein FoldingStaphylococcus aureusRotationMolecular Dynamics SimulationKinetic energyForce field (chemistry)Protein Structure SecondaryArticleMolecular dynamicsMiceProtein structureBacterial ProteinsComputational chemistryAnimalsStatistical physicsPhysical and Theoretical ChemistryMassively parallelQuantitative Biology::BiomoleculesPrincipal Component AnalysisModels StatisticalChemistryProteinsMicrosecondKineticsBundleSolventsThermodynamicsProtein foldingTranscriptional Elongation FactorsCarrier ProteinsAlgorithmsProtein BindingThe journal of physical chemistry. A
researchProduct

Novel avidin-like protein from a root nodule symbiotic bacterium, Bradyrhizobium japonicum.

2005

Bradyrhizobium japonicum is an important nitrogenfixing symbiotic bacterium, which can form root nodules on soybeans. These bacteria have a gene encoding a putative avidin- and streptavidin-like protein, which bears an amino acid sequence identity of only about 30% over the core regions with both of them. We produced this protein in Escherichia coli both as the full-length wild type and as a C-terminally truncated core form and showed that it is indeed a high affinity biotin-binding protein that resembles (strept)avidin structurally and functionally. Because of the considerable dissimilarity in the amino acid sequence, however, it is immunologically very different, and polyclonal rabbit and…

Protein familyProtein ConformationMolecular Sequence DataBiotinmedicine.disease_causeBiochemistryBacterial ProteinsmedicineAnimalsHumansAmino Acid SequenceBradyrhizobiumAntigensMolecular BiologyGeneEscherichia coliPeptide sequencebiologyCell Biologybiology.organism_classificationAvidinBiochemistryPolyclonal antibodiesbiology.proteinRabbitsCarrier ProteinsSequence AlignmentBacteriaBradyrhizobium japonicumAvidinThe Journal of biological chemistry
researchProduct