Search results for "InSe"

showing 10 items of 3069 documents

Impact of maize mucilage on atrazine mineralization andatzC abundance

2005

Soil was amended with maize mucilage, a major rhizodeposit, to study its role on the number of culturable soil micro-organisms, the structure of the bacterial community, atrazine mineralization and atzC abundance. The maximal percentage of atrazine mineralization was lower for mucilage-amended than for water-amended soil. Total culturable soil bacteria and 16S rDNA copy number, measured by RT-PCR, presented similar values and were not significantly (P < 0.05) different among treatments. Mucilage applied at a rate of 70 mu g C g(-1) dry soil day(-1) over two weeks did not modify the abundance of the total soil microflora. Global structure of soil bacterial communities revealed by RISA analys…

DNA Bacterial[SDV]Life Sciences [q-bio]AmendmentBiologyZea mayscomplex mixturesAmidohydrolaseschemistry.chemical_compoundBacterial ProteinsAdhesivesSoil PollutantsPoaceaeAtrazinereal-time pcrSoil MicrobiologymucilageBacteriaHerbicidesPesticide ResiduesBiodiversityGeneral MedicineMineralization (soil science)Biodegradation EnvironmentalMucilagechemistryAgronomyatzc geneInsect Science[SDE]Environmental SciencesSoil waterSoil PollutantsAgronomy and Crop ScienceSoil microbiologyatrazinePest Management Science
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How Does Tremblaya princeps Get Essential Proteins from Its Nested Partner Moranella endobia in the Mealybug Planoccocus citri?

2013

International audience; Many insects maintain intracellular mutualistic symbiosis with a wide range of bacteria which are considered essential for their survival (primary or P-endosymbiont) and typically suffer drastic genome degradation. Progressive loss of P-endosymbiont metabolic capabilities could lead to the recruitment of co-existent facultative endosymbiont (secondary or S-endosymbiont), thus adding more complexity to the symbiotic system. Planococcus citri, among other mealybug species, harbors an unconventional nested endosymbiotic system where every Tremblaya princeps cell (beta-proteobacterium) harbors many Moranella endobia cells (gamma-proteobacterium). In this system, T. princ…

DNA Bacterial[SDV]Life Sciences [q-bio]Planococcus Insectlcsh:MedicineGenomeBacterial genetics03 medical and health sciencesBacterial ProteinsGenome SizeSymbiosisPlanococcus citriAnimalsSymbiosislcsh:ScienceGenome size030304 developmental biologyGenetics0303 health sciencesMultidisciplinarybiology030306 microbiologyHost (biology)lcsh:RBetaproteobacteriaMolecular Sequence AnnotationProkaryoteGene Expression Regulation BacterialSequence Analysis DNAbiology.organism_classificationProtein TransportEssential genelcsh:QGammaproteobacteriaGenome BacterialResearch ArticlePLoS ONE
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Experimental conditions affect the site of tetrazolium violet reduction in the electron transport chain of Lactococcus lactis

2009

The reduction of tetrazolium salts to coloured formazans is often used as an indicator of cell metabolism during microbiology studies, although the reduction mechanisms have never clearly been established in bacteria. The objective of the present study was to identify the reduction mechanisms of tetrazolium violet (TV) in Lactococcus lactis using a mutagenesis approach, under two experimental conditions generally applied in microbiology: a plate test with growing cells, and a liquid test with non-growing (resting) cells. The results showed that in both tests, TV reduction resulted from electron transfer from an intracellular donor (mainly NADH) to TV via the electron transport chain (ETC), …

DNA Bacterial[SDV]Life Sciences [q-bio]Tetrazolium SaltsMicrobiologyElectron Transport03 medical and health scienceschemistry.chemical_compoundElectron transfer030304 developmental biology0303 health sciencesbiology030306 microbiologyLactococcus lactisNADH dehydrogenaseNADH DehydrogenaseVitamin K 2biology.organism_classificationNADElectron transport chainCulture MediaLactococcus lactisMutagenesis InsertionalMembranechemistryBiochemistryGenes Bacterialbiology.proteinFormazanOxidation-ReductionIntracellularBacteria
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Blattabacteria, the endosymbionts of cockroaches, have small genome sizes and high genome copy numbers.

2008

Summary Blattabacteria are intracellular endosymbionts of cockroaches and primitive termites that belong to the class Flavobacteria and live only in specialized cells in the abdominal fat body of their hosts. In the present study we determined genome sizes as well as genome copy numbers for the endosymbionts of three cockroach species, Blattella germanica, Periplaneta americana and Blatta orientalis. The sole presence of blattabacteria in the fat body was demonstrated by rRNA-targeting techniques. The genome sizes of the three blattabacteria were determined by pulsed field gel electrophoresis. The resulting total genome sizes for the three symbionts were all approximately 650 15 kb. Compari…

DNA Bacterialanimal structuresmedia_common.quotation_subjectFat BodyCockroachesInsectBiologyMicrobiologyGenomechemistry.chemical_compoundbiology.animalAnimalsPeriplanetaEcology Evolution Behavior and SystematicsIn Situ Hybridizationmedia_commonGeneticsCockroachBacteroidetesIntracellular parasitefungiBlattaBacteroidetesBlattellidaebiology.organism_classificationElectrophoresis Gel Pulsed-FieldchemistryDNAGenome BacterialPeriplanetaEnvironmental microbiology
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Arginine kinase in the demosponge Suberites domuncula:regulation of its expression and catalytic activity by silicic acid

2005

SUMMARY In Demospongiae (phylum Porifera) the formation of the siliceous skeleton,composed of spicules, is an energetically expensive reaction. The present study demonstrates that primmorphs from the demosponge Suberites domuncula express the gene for arginine kinase after exposure to exogenous silicic acid. The deduced sponge arginine kinase sequence displays the two characteristic domains of the ATP:guanido phosphotransferases; it can be grouped to the `usual' mono-domain 40 kDa guanidino kinases (arginine kinases). Phylogenetic studies indicate that the metazoan guanidino kinases evolved from this ancestral sponge enzyme; among them are also the `unusual'two-domain 80 kDa guanidino kinas…

DNA ComplementaryArgininePhysiologyMolecular Sequence DataSilicic AcidAquatic ScienceCatalysisGene Expression Regulation EnzymologicEvolution Molecularchemistry.chemical_compoundDemospongeMicroscopy Electron TransmissionAnimalsCluster AnalysisAmino Acid SequenceNorthern blotSilicic acidMolecular BiologyIn Situ HybridizationPhylogenyEcology Evolution Behavior and Systematicschemistry.chemical_classificationBase SequencebiologyKinaseArginine KinaseSequence Analysis DNAArginine kinaseBlotting Northernbiology.organism_classificationPoriferaSuberites domunculaEnzymechemistryBiochemistryInsect Sciencebiology.proteinAnimal Science and ZoologySequence AlignmentJournal of Experimental Biology
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A cluster of cuticle protein genes of Drosophila melanogaster at 65A: sequence, structure and evolution

1997

0016-6731 (Print) Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.; A 36-kb genomic DNA segment of the Drosophila melanogaster genome containing 12 clustered cuticle genes has been mapped and partially sequenced. The cluster maps at 65A 5-6 on the left arm of the third chromosome, in agreement with the previously determined location of a putative cluster encompassing the genes for the third instar larval cuticle proteins LCP5, LCP6 and LCP8. This cluster is the largest cuticle gene cluster discovered to date and shows a number of surprising features that explain in part the genetic complexity of the LCP5, LCP6 and LCP8 loci. The genes encoding LCP5 a…

DNA ComplementaryEvolutionMolecular Sequence DataGene DosageSequence HomologyArthropod cuticleInvestigationsGenomeEvolution MolecularSequence Homology Nucleic AcidComplementaryGene clusterGeneticsAnimalsDrosophila melanogaster/*geneticsGene conversionGeneCuticle (hair)GeneticsGenomebiologyNucleic AcidBase SequenceIntronMolecularDNAbiology.organism_classificationInsect Proteins/*geneticsDrosophila melanogasterMultigene FamilyInsect ProteinsDrosophila melanogaster
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Diversity of stonefly hexamerins and implication for the evolution of insect storage proteins

2007

Hexamerins are large storage proteins of insects in the 500 kDa range that evolved from the copper-containing hemocyanins. Hexamerins have been found at high concentration in the hemolymph of many insect taxa, but have remained unstudied in relatively basal taxa. To obtain more detailed insight about early hexamerin evolution, we have studied hexamerins in stoneflies (Plecoptera). Stoneflies are also the only insects for which a functional hemocyanin is known to co-occur with hexamerins in the hemolymph. Here, we identified hexamerins in five plecopteran species and obtained partial cDNA sequences from Perla marginata (Perlidae), Nemoura sp. (Nemouridae), Taeniopteryx burksi (Taeniopterygid…

DNA ComplementaryInsectaMolecular Sequence DataZoologyPerlidaeBiochemistryEvolution MolecularSequence Analysis ProteinPhylogeneticsBotanyHemolymphAnimalsCapniidaeAmino Acid SequenceCloning MolecularMolecular clockMolecular BiologyPhylogenyTaeniopterygidaebiologyPhylogenetic treeSequence Analysis DNANemouridaebiology.organism_classificationInsect ScienceInsect ProteinsSequence AlignmentInsect Biochemistry and Molecular Biology
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Molecular characterization of hemocyanin and hexamerin from the firebrat Thermobia domestica (Zygentoma).

2008

Hexapods possess a tracheal system that enables the transport of oxygen to the inner organs. Although respiratory proteins have been considered unnecessary in most Hexapoda for this reason, we recently showed the presence of a functional hemocyanin in the stonefly Perla marginata. Here we report the identification and molecular characterization of a hemocyanin from Zygentoma (Thysanura). We obtained the full length cDNA of two distinct subunit types from the firebrat Thermobia domestica, and partial sequences of the orthologs from the silverfish Lepisma saccharina. The native T. domestica hemocyanin subunits both consist of 658 amino acids, but a signal peptide for transmembrane transport i…

DNA ComplementaryInsectaProtein subunitmedicine.medical_treatmentMolecular Sequence DataBiochemistrychemistry.chemical_compoundSequence Analysis ProteinHemolymphHemolymphAromatic amino acidsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyPhylogenybiologyHemocyaninbiology.organism_classificationThysanuraProtein SubunitschemistryBiochemistryInsect ScienceHemocyaninsInsect ProteinsThermobiaPterygota (plant)FirebratSequence AlignmentInsect biochemistry and molecular biology
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A respiratory hemocyanin from an insect.

2004

Insects possess an elaborate tracheal system that enables transport of gaseous oxygen from the atmosphere directly to the inner organs. Therefore, the presence of specialized oxygen-transport proteins in the circulatory system of insects has been considered generally unnecessary. Here, we show for the first time, to our knowledge, the presence of an ancestral and functional hemocyanin (Hc) in an insect. In the hemolymph of nymphs and adults of the stonefly Perla marginata , a hexameric Hc was identified, which consists of two distinct subunit types of 659 and 655 amino acids. P. marginata Hc displays cooperative oxygen binding with a moderately high oxygen affinity [(half-saturation pressu…

DNA ComplementaryInsectamedicine.medical_treatmentProtein subunitmedia_common.quotation_subjectMolecular Sequence DataInsectBiologyEvolution MolecularCrustaceaHemolymphHemolymphmedicineAnimalsAmino Acid SequenceCloning MolecularNymphPhylogenymedia_commonchemistry.chemical_classificationMultidisciplinaryBase SequenceSequence Homology Amino AcidRespirationHemocyaninBiological SciencesAmino acidRespiratory proteinOxygenProtein SubunitschemistryBiochemistryHemocyaninsInsect ProteinsFemaleOxygen bindingProceedings of the National Academy of Sciences of the United States of America
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Molecular cloning and expression of Tenebrio molitor ultraspiracle during metamorphosis and in vivo induction of its phosphorylation by 20-hydroxyecd…

2000

Using a RT-PCR approach, the Tenebrio molitor homologue of Drosophila Ultraspiracle (TmUSP) was characterized. Its DNA binding domain shows a degree of identity with those of the other insect USPs. However, the ligand binding domain is closer to those of retinoid X receptors. Using an antibody raised against DmUSP, Western blot analysis of proteins from epidermis and other tissues revealed five immunoreactive bands, corresponding to different phosphorylated forms of a unique polypeptide, as shown by lambda-phosphatase treatment. The nuclear form of TmUSP seems unphosphorylated. An in vivo 20-hydroxyecdysone treatment increases considerably and rapidly the phosphorylated forms of TmUSP. This…

DNA ComplementaryMolecular Sequence Data20-HydroxyecdysoneGene ExpressionMolecular cloningBiologychemistry.chemical_compoundWestern blotGene expressionGeneticsmedicineAnimalsDrosophila ProteinsHumansProtein IsoformsAmino Acid SequenceRNA MessengerCloning MolecularPhosphorylationReceptorTenebrioMolecular BiologyEpidermis (botany)medicine.diagnostic_testMetamorphosis BiologicalDNA-binding domainSequence Analysis DNAMolecular biologyCell biologyDNA-Binding ProteinsEcdysteronechemistryInsect SciencePhosphorylationEpidermisTranscription FactorsInsect molecular biology
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