Search results for "Escher"

showing 10 items of 728 documents

Extremely rapid acclimation of Escherichia coli to high temperature over a few generations of a fed-batch culture during slow warming

2014

This study aimed to demonstrate that adequate slow heating rate allows two strains of Escherichia coli rapid acclimation to higher temperature than upper growth and survival limits known to be strain-dependent. A laboratory (K12-TG1) and an environmental (DPD3084) strain of E. coli were subjected to rapid (few seconds) or slow warming (1 degrees C 12 h(-1)) in order to (re) evaluate upper survival and growth limits. The slow warming was applied from the ancestral temperature 37 degrees C to total cell death 46-54 degrees C: about 30 generations were propagated. Upper survival and growth limits for rapid warming (46 degrees C) were lower than for slow warming (46-54 degrees C). The thermal l…

Hot TemperatureMembrane FluidityAcclimatizationslow warmingBiologymedicine.disease_causeMicrobiologyAcclimatizationProtein Structure SecondaryHot Temperature03 medical and health sciencesAcclimation;Escherichia coli;slow warming;thermal nicheBotanymedicineEscherichia coli[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringEscherichia coliOriginal Research030304 developmental biologyBacteriological Techniques0303 health sciencesStrain (chemistry)030306 microbiologyEscherichia coli ProteinsTotal cellBacterial LoadFed-batch cultureBatch Cell Culture Techniques13. Climate actionBiophysicsThermal limitthermal nicheRandom mutationAcclimation
researchProduct

Amino acid substitutions enhancing thermostability of Bacillus polymyxa beta-glucosidase A

1996

Mutations enhancing the thermostability of β-glucosidase A of Bacillus polymyxa, a family 1 glycosyl hydrolase, have been obtained after hydroxylamine mutagenesis of a plasmid containing the bglA gene, transformation of Escherichia coli with the mutagenized plasmid, and identification of transformant colonies that showed β-glucosidase activity after a thermal treatment that inactivated the wild-type enzyme. Two additive mutations have been characterized that cause replacement of glutamate at position 96 by lysine and of methionine at position 416 by isoleucine respectively. The thermoresistant mutant enzymes showed increased resistance to other denaturing agents, such as pH and urea, while …

Hot TemperatureMutantMolecular Sequence DataBacillusHydroxylamineBiologymedicine.disease_causeHydroxylaminesBiochemistryProtein Structure Secondarychemistry.chemical_compoundHydrolaseEnzyme StabilitymedicineEscherichia coliPoint MutationAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliThermostabilitychemistry.chemical_classificationMethionineBase Sequencebeta-GlucosidaseCell BiologyMolecular biologyRecombinant ProteinsAmino acidKineticschemistryBiochemistryOligodeoxyribonucleotidesMutagenesisMutagenesis Site-DirectedThermodynamicsSpectrophotometry UltravioletIsoleucineCysteineResearch Article
researchProduct

Chip calorimetry for the monitoring of whole cell biotransformation

2005

Abstract Efficient control of whole cell biotransformation requires quantitative real-time information about the thermodynamics and kinetics of growth and product formation. Heat production contains such information, but its technical application is restricted due to the high price of calorimetric devices, the difficulty of integrating them into existing bioprocesses and the slow response times of established microcalorimeters. A new generation of chip or nanocalorimeters may overcome these weaknesses. We thus tested a highly sensitive chip calorimeter for its applicability in biotechnological monitoring. It was used to monitor aerobic growth of suspended and immobilized Escherichia coli DH…

Hot TemperatureTime FactorsAnalytical chemistryBioengineeringCalorimetryCalorimetryModels BiologicalApplied Microbiology and BiotechnologyBiotransformationEscherichia coliProcess controlAnaerobiosisBioprocessProcess engineeringBiotransformationCells CulturedChemistrybusiness.industryGeneral MedicineChipCalorimeterKineticsThermodynamicsHalomonasbusinessWhole cellBiosensorBiotechnologyJournal of Biotechnology
researchProduct

Effect of pasteurization on the bactericidal capacity of human milk.

2008

The use of human milk in milk banks requires thermal processing to eliminate microbiological hazards. An evaluation is made of the stability of overall human milk bactericidal capacity following 2 modalities of thermal pasteurization: 63°C/30 minutes and 75°C/15 seconds. Ten milk samples (mature milk) were analyzed. In each sample, the effect of both thermal treatments on bactericidal capacity against Escherichia coli was evaluated in relation to the capacity of fresh milk (control). All the samples analyzed possessed bactericidal capacity. Human milk pasteurization induced a significant loss of this capacity that was more pronounced after high-temperature treatment than after low-temperat…

Hot TemperatureTime FactorsMilk HumanChemistryFood HandlingColony Count Microbialfood and beveragesObstetrics and GynecologyPasteurizationAntimicrobiallaw.inventionMicrobiologyAnti-Bacterial AgentsFresh milkfluids and secretionsMilk BankslawEscherichia coliHumansFemaleFood scienceMilk BanksMature milkJournal of human lactation : official journal of International Lactation Consultant Association
researchProduct

Nouvelles perspectives concernant la structure et la fonction du domaine carboxyl terminal de Hfq

2015

Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA). The Escherichia coli Hfq is structurally organized into two domains. An N-terminal domain that folds as strongly bent β-sheets within individual protomers to…

IDP intrinsically-disordered proteinslcsh:Lifelcsh:QR1-502sub-membrane macromolecular assemblyPlasma protein bindingsRNA small non-coding RNABiochemistrylcsh:Microbiologyamyloid fibrilsProtein biosynthesis0303 health sciences[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Escherichia coli Proteins030302 biochemistry & molecular biologyHfqCTRp Hfq C-terminal peptideFTIR Fourier transform infrared spectroscopyNTR N-terminal regionCompartmentalization (psychology)Cell biology[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsRNA Bacterialsmall non-coding ribonucleic acid (RNA)BiochemistryFSD Fourier self-deconvolutionTransfer RNAAmyloid fibrilProtein BindingBiophysicsBiologyHost Factor 1 Protein03 medical and health sciencesEscherichia coliThT thioflavin T[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein Structure QuaternaryncRNA regulatory non-coding RNAPost-transcriptional regulationMolecular Biology030304 developmental biologyOriginal PaperC-terminusRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyCell Biologycellular compartmentalizationWT wild-typeProtein Structure Tertiarylcsh:QH501-531Host Factor 1 ProteinCTR Hfq C-terminal regionribonucleic acid (RNA) processing and degradationBiophysicpost-transcriptional regulationBioscience Reports
researchProduct

Mutilation of RNA phage Qβ virus-like particles: from icosahedrons to rods

2000

Icosahedral virus-like particles (VLPs) of RNA phage Qbeta are stabilized by four disulfide bonds of cysteine residues 74 and 80 within the loop between beta-strands F and G (FG loop) of the monomeric subunits, which determine the five-fold and quasi-six-fold symmetry contacts of the VLPs. In order to reduce the stability of Qbeta VLPs, we mutationally converted the amino acid stretch 76-ANGSCD-81 within the FG loop into the 76-VGGVEL-81 sequence. It led to production in Escherichia coli cells of aberrant rod-like Qbeta VLPs, along with normal icosahedral capsids. The length of the rod-like particles exceeded 4-30 times the diameter of icosahedral Qbeta VLPs.

Icosahedral symmetryvirusesGenetic VectorsMolecular Sequence DataBiophysicsBiologymedicine.disease_causecomplex mixturesBiochemistryVirus-like particleStructural BiologyGeneticsmedicineAmino Acid SequenceCysteineMolecular BiologyEscherichia coliPeptide sequenceIcosahedronAlloleviviruschemistry.chemical_classificationSequence Homology Amino AcidRod-like structureVirionvirus diseasesRNASelf-assemblyCell Biologybiochemical phenomena metabolism and nutritionAmino acidCrystallographyCapsidchemistryMutagenesis Site-DirectedRNA ViralRNA phage QβVirus-like particleCysteineFEBS Letters
researchProduct

Identification of modifications in microbial, native tRNA that suppress immunostimulatory activity

2012

2′-O-methylation of guanosine 18 is a naturally occurring tRNA modification that can suppress immune TLR7 responses.

ImmunologyMutantfungiBrief Definitive ReportRNAfood and beveragesvirus diseasesContext (language use)Biologybiochemical phenomena metabolism and nutritionmedicine.disease_causeTRNA MethyltransferasesTransplantationchemistry.chemical_compoundBiochemistrychemistryTransfer RNAmedicineImmunology and AllergyEscherichia coliDNAThe Journal of Experimental Medicine
researchProduct

Cell surface display of rat invariant γ chain: detection by monoclonal antibodies directed against a C-terminal γ chain segment

1992

A series of 14 monoclonal antibodies (mAb) directed against the C-terminal part of the rat invariant gamma chain (amino acid 142-216) was generated using distinct fusion proteins that contain this gamma segment for immunization and hybridoma screening. Additional fusion protein were prepared carrying discrete regions of the gamma chain. Employing these reagents confirmed that the obtained mAb do indeed recognize the C-terminal portion of the invariant chain, as demonstrated by Western blot analysis. All mAb established recognize epitopes present on the native gamma chain, as revealed by immunoprecipitation analysis using nonionic detergent extracts of metabolically labeled Lewis rat splenoc…

Immunoprecipitationmedicine.drug_classRecombinant Fusion ProteinsBlotting WesternGenetic VectorsImmunologyMonoclonal antibodyEpitopeMiceWestern blotEscherichia colimedicineAnimalsImmunology and AllergyElectrophoresis Gel Two-DimensionalCloning MolecularGel electrophoresisMice Inbred BALB CHybridomasbiologymedicine.diagnostic_testHistocompatibility Antigens Class IIAntibodies MonoclonalFlow CytometryFusion proteinPrimary and secondary antibodiesMolecular biologyRatsAntigens Differentiation B-LymphocyteBiochemistryRats Inbred LewAntigens Surfacebiology.proteinAntibodySpleenPlasmidsEuropean Journal of Immunology
researchProduct

The evolution of the heat-shock protein GroEL from Buchnera, the primary endosymbiont of aphids, is governed by positive selection

2002

The heat-shock protein GroEL is a double-ring-structured chaperonin that assists the folding of many newly synthesized proteins in Escherichia coli and the refolding in vitro, with the cochaperonin GroES, of conformationally damaged proteins. This protein is constitutively overexpressed in the primary symbiotic bacteria of many insects, constituting approximately 10% of the total protein in Buchnera, the primary endosymbiont of aphids. In the present study, we perform a maximum likelihood (ML) analysis to unveil the selective constraints in GroEL. In addition, we apply a new statistical approach to determine the patterns of evolution in this highly interesting protein. The main conclusion d…

In Vitro Techniquesmedicine.disease_causePolymerase Chain ReactionChaperoninEvolution MolecularBuchneraHeat shock proteinOperonEscherichia coliGeneticsmedicineAnimalsCell LineageSelection GeneticSymbiosisMolecular BiologyEscherichia coliPhylogenyEcology Evolution Behavior and SystematicsDNA PrimersGeneticsbiologyPhylogenetic treeChaperonin 60GroESbiochemical phenomena metabolism and nutritionbiology.organism_classificationGroELAmino Acid SubstitutionAphidsbacteriaBuchneraSymbiotic bacteria
researchProduct

2,6-Disubstituted imidazo[2,1-b][1,3,4]thiadiazole derivatives as potent staphylococcal biofilm inhibitors.

2019

Abstract A class of 36 new 2-(6-phenylimidazo[2,-1-b][1,3,4]thiadiazol-2-yl)-1H-indoles was efficiently synthesized and evaluated for their anti-biofilm properties against the Gram-positive bacterial reference strains Staphylococcus aureus ATCC 25923, S. aureus ATCC 6538 and Staphylococcus epidermidis ATCC 12228, and the Gram-negative strains Pseudomonas aeruginosa ATCC 15442 and Escherichia coli ATCC 25922. Many of these new compounds, were able to inhibit biofilm formation of the tested staphylococcal strains showing BIC50 lower than 10 μg/ml. In particular, derivatives 9c and 9h showed remarkable anti-biofilm activity against S. aureus ATCC 25923 with BIC50 values of 0.5 and 0.8 μg/ml, r…

Indoles3Anti-virulence agentStaphylococcus1-b][1Bacterial growthAnti-Biofilm agentsmedicine.disease_causeSettore BIO/19 - Microbiologia GeneraleGram-Positive Bacteriaimidazo[201 natural sciencesVirulence factorMicrobiology03 medical and health sciencesStaphylococcus epidermidisDrug DiscoveryGram-Negative BacteriaThiadiazolesmedicineStaphylococcal biofilm inhibitorsEscherichia coli030304 developmental biologyPharmacology0303 health sciences4]thiadiazole derivativesbiologyStaphylococcal biofilm inhibitorVirulenceAnti-Biofilm agents; Anti-virulence agents; imidazo[21-b][134]thiadiazole derivatives; Staphylococcal biofilm inhibitors; Anti-Bacterial Agents; Biofilms; Gram-Negative Bacteria; Gram-Positive Bacteria; Indoles; Staphylococcus; Thiadiazoles; Virulence010405 organic chemistryPseudomonas aeruginosaChemistryimidazo[21-b][134]thiadiazole derivativesOrganic ChemistryBiofilmGeneral Medicinebiology.organism_classificationSettore CHIM/08 - Chimica FarmaceuticaAnti-Biofilm agent0104 chemical sciencesAnti-Bacterial AgentsAnti-virulence agentsStaphylococcus aureusBiofilms1 3 4 thiadiazole derivativesEuropean journal of medicinal chemistry
researchProduct