Search results for "Bacterial proteins"

showing 10 items of 614 documents

Functional significance of membrane associated proteolysis in the toxicity of Bacillus thuringiensis Cry3Aa toxin against Colorado potato beetle.

2012

Abstract Bacillus thuringiensis Cry toxins are widely used as biocontrol agents in bioinsecticides and transgenic plants. In the three domain-Cry toxins, domain II has been identified as an important determinant of their highly specific activity against insects. In this work, we assessed the role in membrane associated proteolysis and toxicity in Colorado potato beetle (CPB) of a previously reported ADAM recognition motif present in Cry3Aa toxin domain II. We used site-directed mutagenesis to modify the Bacillus thuringiensis cry3A gene in amino acid residues 344, 346, 347, 351 and 353 of the ADAM recognition motif in Cry3Aa toxin. Cry3Aa toxin mutants displayed decreased toxicity when comp…

ProteasesColoradoProteolysisMutantBacillus thuringiensisToxicologymedicine.disease_causeMicrobiologyHemolysin ProteinsRecognition sequenceBacterial ProteinsBacillus thuringiensismedicineAnimalsAmino Acid SequencePest Control BiologicalCells Culturedbiologymedicine.diagnostic_testBacillus thuringiensis ToxinsMicrovilliToxinfungiColorado potato beetleWild typeSequence Analysis DNAbiology.organism_classificationColeopteraEndotoxinsBiochemistryProteolysisMutagenesis Site-DirectedToxicon : official journal of the International Society on Toxinology
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Prohibitin, an essential protein for Colorado potato beetle larval viability, is relevant to Bacillus thuringiensis Cry3Aa toxicity

2013

Bacillus thuringienesis (Bt) Cry toxins constitute the most extensively used environmentally safe biopesticide and their mode of action relies on the interaction of the toxins with membrane proteins in the midgut of susceptible insects that mediate toxicity and insect specificity. Therefore, identification of Bt Cry toxin interacting proteins in the midgut of target insects and understanding their role in toxicity is of great interest to exploit their insecticidal action. Using ligand blot, we demonstrated that Bt Cry3Aa toxin bound to a 30kDa protein in Colorado potato beetle (CPB) larval midgut membrane, identified by sequence homology as prohibitin-1 protein. Prohibitins comprise a highl…

ProteasesHealth Toxicology and MutagenesisBiologymedicine.disease_causeHemolysin ProteinsBacterial ProteinsRNA interferenceBacillus thuringiensisProhibitinsmedicineAnimalsProhibitinBinding siteMode of actionSolanum tuberosumBacillus thuringiensis ToxinsToxinfungiGeneral Medicinebiology.organism_classificationMolecular biologyColeopteraEndotoxinsRepressor ProteinsMembrane proteinBiochemistryLarvaAgronomy and Crop SciencePesticide Biochemistry and Physiology
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Characterization of EprA, a major extracellular protein of Oenococcus oeni with protease activity

2008

International audience; Extracellular proteins from Oenococcus oeni. a wine-making bacterium, were isolated during growth on media differing by their nitrogen content. Analysis by two-dimensional electrophoresis revealed a low number of protein signals. Among the main spots, one signal corresponded to a single protein, which contained a lysine repeat domain characteristic of cell-wall hydrolases. We demonstrated that this major protein, named EprA, was able to hydrolyse several proteins. The heterologous production of this protein in Escherichia coli confirmed the protease activity of EprA. With a MW of 21.3 kDa and a pl of 5.3, EprA presents optimal activity at pH 7.0 and 45 degrees C. Thi…

ProteasesHydrolyzed proteinNitrogenmedicine.medical_treatmentWinemedicine.disease_causeMicrobiology[ CHIM ] Chemical SciencesMicrobiology03 medical and health sciencesBacterial Proteinsmedicine[CHIM]Chemical SciencesElectrophoresis Gel Two-DimensionalPolyacrylamide gel electrophoresisEscherichia coli030304 developmental biologyOenococcus oenichemistry.chemical_classification0303 health sciencesProteasebiology030306 microbiologyTemperatureGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationCulture MediaMolecular WeightEnzymeBiochemistrychemistryFermentationFood MicrobiologyElectrophoresis Polyacrylamide GelOenococcusLeuconostocFood SciencePeptide Hydrolases
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Investigation of the steps involved in the difference of susceptibility of Ephestia kuehniella and Spodoptera littoralis to the Bacillus thuringiensi…

2011

BUPM95 is a Bacillus thuringiensis subsp. kurstaki strain producing the Vip3Aa16 toxin with an interesting insecticidal activity against the Lepidopteran larvae Ephestia kuehniella. Study of different steps in the mode of action of this Vegetative Insecticidal Protein on the Mediterranean flour moth (E. kuehniella) was carried out in the aim to investigate the origin of the higher susceptibility of this insect to Vip3Aa16 toxin compared to that of the Egyptian cotton leaf worm Spodoptera littoralis. Using E. kuehniella gut juice, protoxin proteolysis generated a major band corresponding to the active toxin and another band of about 22kDa, whereas the activation of Vip3Aa16 by S. littoralis …

ProteasesProteolysismedia_common.quotation_subjectBacillus thuringiensisDrug ResistanceActivationBacillusInsectMothsSpodopteraBiologymedicine.disease_causeMicrobiologyBacterial ProteinsVip3Aa16Bacillus thuringiensismedicineAnimalsPest Control BiologicalSpodoptera littoralisEcology Evolution Behavior and SystematicsEphestia kuehniellamedia_commonmedicine.diagnostic_testToxinfungiSpodoptera littoralisbiology.organism_classificationMediterranean flour mothLarvaBacillusthuringiensisMidgut putative receptorJournal of Invertebrate Pathology
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Broad Spectrum Thiopeptide Recognition Specificity of theStreptomyces lividans TipAL Protein and Its Role in Regulating Gene Expression

1999

Microbial metabolites isolated in screening programs for their ability to activate transcription of the tipA promoter (ptipA) in Streptomyces lividans define a class of cyclic thiopeptide antibiotics having dehydroalanine side chains ("tails"). Here we show that such compounds of heterogeneous primary structure (representatives tested: thiostrepton, nosiheptide, berninamycin, promothiocin) are all recognized by TipAS and TipAL, two in-frame translation products of the tipA gene. The N-terminal helix-turn-helix DNA binding motif of TipAL is homologous to the MerR family of transcriptional activators, while the C terminus forms a novel ligand-binding domain. ptipA inducers formed irreversible…

Protein ConformationMolecular Sequence DataMutantBiologyBiochemistryStreptomycesMass SpectrometryThiostreptonchemistry.chemical_compoundProtein structureBacterial ProteinsDehydroalanineAmino Acid SequenceMolecular BiologyRegulation of gene expressionAlanineProtein primary structureGene Expression Regulation BacterialCell Biologybiology.organism_classificationStreptomycesAnti-Bacterial AgentschemistryBiochemistryTrans-ActivatorsPeptidesNosiheptideJournal of Biological Chemistry
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Biotechnical applications of small heat shock proteins from bacteria.

2012

The stress responses of most bacteria are thought to involve the upregulation of small heat shock proteins. We describe here some of the most pertinent aspects of small heat shock proteins, to highlight their potential for use in various applications. Bacterial species have between one and 13 genes encoding small heat shock proteins, the precise number depending on the species considered. Major efforts have recently been made to characterize the protein protection and membrane stabilization mechanisms involving small heat shock proteins in bacteria. These proteins seem to be involved in the acquisition of cellular heat tolerance. They could therefore potentially be used to maintain cell via…

Protein FoldingHeterologousmedicine.disease_causeBiochemistryMicrobiologyDownregulation and upregulationBacterial ProteinsStress PhysiologicalHeat shock proteinmedicineHumansViability assayEscherichia coliInclusion BodiesbiologyProtein StabilityProbioticsCell Biologybiology.organism_classificationRecombinant ProteinsCell biologyHeat-Shock Proteins SmallSolubilityShock (circulatory)Food TechnologyProtein foldingmedicine.symptomBacteriaBiotechnologyThe international journal of biochemistrycell biology
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Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection.

2019

The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD+ sodium-translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn2+ by the His51, His55, His140 residues, and the Zn2+ -binding site indicates that BB0365 could act as a potential metalloenzyme; therefore…

Protein FoldingProtein ConformationLipoproteinsBiophysicsBiochemistryMicrobiology03 medical and health sciencesLyme diseaseBacterial ProteinsStructural BiologyOxidoreductaseGeneticsmedicineHumansBinding siteBorrelia burgdorferiMolecular BiologyFerredoxin030304 developmental biologychemistry.chemical_classification0303 health sciencesLyme DiseaseBinding SitesbiologyChemistry030302 biochemistry & molecular biologyCell BiologyPeriplasmic spacebacterial infections and mycosesmedicine.diseasebiology.organism_classificationZincMembrane proteinBorrelia burgdorferiPeriplasmbacteriaNAD+ kinaseSodium-Potassium-Exchanging ATPaseFEBS lettersReferences
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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
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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
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A Genomic, Transcriptomic and Proteomic Look at the GE2270 Producer Planobispora rosea, an Uncommon Actinomycete.

2015

We report the genome sequence of Planobispora rosea ATCC 53733, a mycelium-forming soil-dweller belonging to one of the lesser studied genera of Actinobacteria and producing the thiopeptide GE2270. The P. rosea genome presents considerable convergence in gene organization and function with other members in the family Streptosporangiaceae, with a significant number (44%) of shared orthologs. Patterns of gene expression in P. rosea cultures during exponential and stationary phase have been analyzed using whole transcriptome shotgun sequencing and by proteome analysis. Among the differentially abundant proteins, those involved in protein metabolism are particularly represented, including the G…

ProteomeSequence analysislcsh:MedicineGenomicsBiologyGenomePeptides Cyclic03 medical and health sciencesBacterial ProteinsPlanobispora roseaActinomycetalesGenomic libraryAgricultural and Biological Sciences (all); Biochemistry Genetics and Molecular Biology (all); Medicine (all)lcsh:ScienceGeneProteomic Look030304 developmental biologyWhole genome sequencingGenetics0303 health sciencesMultidisciplinaryBiochemistry Genetics and Molecular Biology (all)030306 microbiologyShotgun sequencingSequence Analysis RNAMedicine (all)lcsh:RUncommon Actinomycete.High-Throughput Nucleotide SequencingGenomicsRNA BacterialThiazolesGlucoseTranscriptomicAgricultural and Biological Sciences (all)Multigene FamilyProteomeGenomiclcsh:QTranscriptomeGenome BacterialMetabolic Networks and PathwaysResearch ArticlePLoS ONE
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