Search results for "bacteria."

showing 10 items of 4757 documents

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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Mutational analyses of YqjA, a Tvp38/DedA protein of E. coli

2015

AbstractMembrane proteins of the DedA/Tvp38 protein family are involved in membrane integrity and virulence of pathogenic organisms. However, the structure and exact function of any member of this large protein family are still unclear. In the present study we analyzed the functional and structural properties of a DedA homolog. Purified YqjA variants from Escherichia coli are detectable in different oligomeric states and specific homo-interaction of YqjA monomers in the membrane were confirmed by formation of a disulfide bond in the C-terminal transmembrane helix. Moreover, alanine scanning mutagenesis exhibited different interaction sites crucial for YqjA activity vs. dimer formation.

Protein familyDNA Mutational AnalysisBiophysicsVirulencelac operonmedicine.disease_causeBiochemistryProtein Structure SecondaryTvp38Structural BiologyEscherichia coliGeneticsmedicineOligomerizationFunctionMolecular BiologyEscherichia coliAlanineChemistryEscherichia coli ProteinsCell MembraneMutagenesisMembrane ProteinsGene Expression Regulation BacterialCell BiologyAlanine scanningTransmembrane domainMembrane proteinBiochemistryDedAMembrane proteinMutationProtein MultimerizationFEBS Letters
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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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Pathogens and host immunity in the ancient human oral cavity.

2014

Calcified dental plaque (dental calculus) preserves for millennia and entraps biomolecules from all domains of life and viruses. We report the first high-resolution taxonomic and protein functional characterization of the ancient oral microbiome and demonstrate that the oral cavity has long served as a reservoir for bacteria implicated in both local and systemic disease. We characterize: (i) the ancient oral microbiome in a diseased state, (ii) 40 opportunistic pathogens, (iii) the first evidence of ancient human-associated putative antibiotic resistance genes, (iv) a genome reconstruction of the periodontal pathogen Tannerella forsythia, (v) 239 bacterial and 43 human proteins, allowing co…

ProteomeMolecular Sequence Data610 Medicine & health10071 Functional Genomics Center ZurichDental plaqueArticlePrehistòriaBacterial geneticsPeriodontal pathogenMicrobiology1311 GeneticsTandem Mass SpectrometryGermanyRNA Ribosomal 16SGeneticsmedicineTannerella forsythiaHumansDental CalculusMicrobiomePathogenPhylogenyMouthbiologyBase SequenceEcologyBacteroidetesMicrobiotaSequence Analysis DNAbiology.organism_classificationmedicine.diseaseRed complexHistory Medieval10182 Institute of Oral Biologystomatognathic diseasesArchaeology10076 Center for Integrative Human Physiology11294 Institute of Evolutionary Medicine570 Life sciences; biologyOral MicrobiomeFood AnalysisGenome BacterialNature genetics
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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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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
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Reading the Evolution of Compartmentalization in the Ribosome Assembly Toolbox: The YRG Protein Family.

2016

Reconstructing the transition from a single compartment bacterium to a highly compartmentalized eukaryotic cell is one of the most studied problems of evolutionary cell biology. However, timing and details of the establishment of compartmentalization are unclear and difficult to assess. Here, we propose the use of molecular markers specific to cellular compartments to set up a framework to advance the understanding of this complex intracellular process. Specifically, we use a protein family related to ribosome biogenesis, YRG (YlqF related GTPases), whose evolution is linked to the establishment of cellular compartments, leveraging the current genomic data. We analyzed orthologous proteins …

ProteomesArchaeal ProteinsMycologyBioenergeticsResearch and Analysis MethodsBiochemistryMicrobiologyMolecular EvolutionGTP PhosphohydrolasesEvolution MolecularFungal ProteinsEukaryotic EvolutionBacterial ProteinsFungal EvolutionAnimalsMolecular Biology TechniquesMolecular BiologyEnergy-Producing OrganellesCell NucleusEvolutionary BiologyMolecular Biology Assays and Analysis TechniquesBacterial EvolutionBiology and Life SciencesProteinsPhylogenetic AnalysisBacteriologyNucleolusCell BiologyOrganismal EvolutionCell CompartmentationMitochondriaProtein TransportMicrobial EvolutionCellular Structures and OrganellesRibosomesResearch ArticlePloS one
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Metaproteomic analysis of atmospheric aerosol samples.

2016

Metaproteomic analysis of air particulate matter provides information about the abundance and properties of bioaerosols in the atmosphere and their influence on climate and public health. We developed and applied efficient methods for the extraction and analysis of proteins from glass fiber filter samples of total, coarse, and fine particulate matter. Size exclusion chromatography was applied to remove matrix components, and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was applied for protein fractionation according to molecular size, followed by in-gel digestion and LC-MS/MS analysis of peptides using a hybrid Quadrupole-Orbitrap MS. Maxquant software and the Swiss-…

Proteomics010504 meteorology & atmospheric sciencesSize-exclusion chromatographyIndoor bioaerosolFractionation010501 environmental sciences01 natural sciencesBiochemistryAnalytical ChemistryMatrix (chemical analysis)Fungal ProteinsBacterial ProteinsMetaproteomicsTandem Mass SpectrometryDatabases ProteinChromatography High Pressure Liquid0105 earth and related environmental sciencesPlant ProteinsAerosolsFungal proteinAir PollutantsChromatographyMass spectrometryChemistryAtmosphereProteinsParticulatesAllergensAtmospheric aerosolsAerosolEnvironmental chemistryBioanalytical methodsParticleElectrophoresis Polyacrylamide GelParticulate MatterHPLCResearch PaperAnalytical and bioanalytical chemistry
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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
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