Search results for "Plants"

showing 10 items of 1914 documents

Synthetic cartography for mapping biodiversity in the Mediterranean region: Sicily as a case study

2018

This paper proposes a new hierarchical land classification system for the mapping of species distribution at national or regional scales. Our integrative framework incorporates two hierarchical levels inferred from historical, climatic, geomorphological and geological attributes. The feasibility of this proposal is based on the use of historical collections and literature data, as well as on its ability to combine old low-precision data with more recent records of higher resolution. The system is set up for vascular plants, but it can also be used for other taxonomic groups. Furthermore, it has the potential for application to the whole Mediterranean region because it is based on informatio…

0106 biological sciencesMediterranean climateCartographyGeographic information systemConservation Biologyspatial analysisSpecies distributionBiodiversity & Conservationdata analysisBiodiversityDistribution (economics)Plant Science010603 evolutionary biology01 natural sciencesRemote Sensing and GISFloristics & DistributionPlant sciencelcsh:BotanydistributionTaxonomic rankEcology Evolution Behavior and Systematicsbiological collectionsbusiness.industryplantsSouthern Europe and MediterraneanData analysiPlantSpecies InventoriesEcology Evolution Behavior and Systematiclcsh:QK1-989GIS softwareGeographyAngiospermaeBiogeographySpatial analysiBiological collectionbusinessCartography010606 plant biology & botanyResearch ArticlePhytoKeys
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Regulation of plant NADPH oxidase.

2007

Addendum to: Regulation of Reactive Oxygen Species Production by a 14-3-3 Protein in Elicited Tobacco Cells. T. Elmayan, J. Fromentin, C. Riondet, G. Alcaraz, J. Blein and F. Simon-Plas. Plant Cell Environ 2007; 30:722–32; International audience; The production of Reactive Oxygen Species (ROS) is one of the key events occurring during the response of plants to environmental changes, and contributing to establish adaptive signaling pathways. A plasma membrane bound NADPH oxidase enzyme has been evidenced as the ROS producing system in various plant‑microorganisms interactions. We very recently reported, that a protein of the 14‑3‑3 family was able to interact directly with the C‑terminus par…

0106 biological sciencesMembrane boundContext (language use)Plant Science01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciences[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsNADPH OXIDASEPlant defense against herbivoryREACTIVE OXYGEN SPECIES14-3-3030304 developmental biologyPROTEINE PHOSPHATASE TYPE 2Cchemistry.chemical_classification0303 health sciencesReactive oxygen speciesOxidase testNADPH oxidasebiologyTWO-HYBRIDArticle AddendumEnzymeBiochemistrychemistryREGULATIONbiology.proteinSignal transduction010606 plant biology & botanyPlant signalingbehavior
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Molecular Bases for Sensitivity to Tubulin-Binding Herbicides in Green Foxtail

2004

Abstract We investigated the molecular bases for resistance to several classes of herbicides that bind tubulins in green foxtail (Setaria viridis L. Beauv.). We identified two α- and two β-tubulin genes in green foxtail. Sequence comparison between resistant and sensitive plants revealed two mutations, a leucine-to-phenylalanine change at position 136 and a threonine-to-isoleucine change at position 239, in the gene encoding α2-tubulin. Association of mutation at position 239 with herbicide resistance was demonstrated using near-isogenic lines derived from interspecific pairings between green foxtail and foxtail millet (Setaria italica L. Beauv.), and herbicide sensitivity bioassays combine…

0106 biological sciencesModels MolecularSetariaPhysiologyProtein ConformationMolecular Sequence DataSetaria PlantDrug ResistancePlant Sciencemedicine.disease_cause01 natural sciencesTubulin binding[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciencesFocus Issue on the Plant CytoskeletonSpecies SpecificityTubulin[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsBotanyGeneticsmedicineBioassayAmino Acid SequenceGeneCross-resistancePhylogenyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesMutationbiologyBase SequenceSetaria viridisHerbicidesbiology.organism_classificationBiochemistryFoxtail010606 plant biology & botanyProtein Binding
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Evidence for a geranyl-diphosphate synthase located within the plastids of Vitis vinifera L. cultivated in vitro

1992

Intact plastids from cell suspensions of Vitis vinifera L. cv. Muscat de Frontignan, free of detectable contamination by other particles as judged by the distribution of organelle-specific marker enzymes and by electron microscopy, exhibit geranyl-diphosphate synthase activity (EC 2.5.1.1). This synthase activity remains stable after tryptic digestion of unlysed organelles and is enhanced by plastid disruption. We conclude that the enzyme is located within the organelle. The possibility of an isopentenyl diphosphate/dimethylallyl diphosphate translocating system which would play a major role in the regulation of monoterpene metabolism is discussed.

0106 biological sciencesMonoterpenePlant Science01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciences[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsOrganelleGeneticsPlastidComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesATP synthasebiologyMetabolismTECHNIQUE DES TRACEURSTerpenoidEnzymeBiochemistrychemistryCULTURE DE CELLULECell culturebiology.protein010606 plant biology & botanyPlanta
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Evidence for specific, high-affinity binding sites for a proteinaceous elicitor in tobacco plasma membrane

1995

Abstract Binding of cryptogein, a proteinaceous elicitor, was studied on tobacco plasma membrane. The binding of the [125I]cryptogein was saturable, reversible and specific with an apparent Kd of 2 nM. A single class of cryptogein binding sites was found with a sharp optimum pH for binding at about pH 7.0. The high-affinity correlates with cryptogein concentrations required for biological activity in vivo.

0106 biological sciencesNicotiana tabacumBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular Biology01 natural sciencesBiochemistryFungal Proteins03 medical and health sciencesStructural BiologyIn vivoTobaccoGeneticsBinding siteReceptor[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesBinding SitesbiologyNicotiana tabacumChemistryAlgal ProteinsCell MembraneElicitinBiological activityCell BiologyElicitorbiology.organism_classification3. Good healthElicitorKineticsPlants ToxicMembraneBiochemistryCryptogeinPlasma membraneReceptor010606 plant biology & botany
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Comparison of the effects of cryptogein and oligogalacturonides on tabacco cells and evidence of different forms of desensitization induced by these …

1998

Abstract The effects of cryptogein and oligogalacturonides (OGs) were compared on tobacco cells by measuring calcium influx and calcium-dependent responses including extracellular alkalinization and H 2 O 2 production. The main difference is the higher calcium influx and the sustained H 2 O 2 production induced by cryptogein compared to OGs. Amplitude and duration of calcium signalling triggered by cryptogein or OGs may explain the necrotic effect of cryptogein, and the absence of necrosis in tobacco plants treated with OGs. We used induction of alkalinization and H 2 O 2 production to investigate cryptogein effects after a first treatment with cryptogein or OGs, and reciprocally. Results s…

0106 biological sciencesNicotiana tabacumchemistry.chemical_elementStimulationPlant ScienceCalciumBiology01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health sciences[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsBotanyGeneticsExtracellularComputingMilieux_MISCELLANEOUS030304 developmental biologyCalcium signaling0303 health sciencesGeneral Medicinebiology.organism_classificationElicitorCell biologyRespiratory burstchemistrySignal transductionAgronomy and Crop Science010606 plant biology & botany
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No apparent effect of invasive alien goldenrod on soil microbial communities or soil fauna feeding activity

2020

Abstract Invasive alien species spreading in abandoned agricultural landscape may negatively affect native organisms, including plants and soil biota. This study assessed the effects of invasion by Solidago sp. (goldenrod) in southern Poland on soil fauna feeding activity and on soil microorganism activity, biomass, and functional and taxonomic diversity, in a comparisons of paired plots: goldenrod-invaded plots and nearby non-invaded plots of semi-natural grassland. Goldenrod-invaded plots had fewer vascular plant species (paired t-test) than non-invaded ones, and showed a distinct plant community composition (ANOSIM). Non-invaded and invaded plots did not differ in a range of measured soi…

0106 biological sciencesOTUSoil biologyBiodiversityBeta diversitySolidago altissimaAlien speciesalien speciesMicrobial functional diversity010603 evolutionary biology01 natural sciencesbiological diversityvascular plantsEcology Evolution Behavior and SystematicsNature and Landscape ConservationBiomass (ecology)biologyEcologyVascular plantsIllumina sequencingPlant community04 agricultural and veterinary sciencesbiology.organism_classificationBiological diversityMicrobial population biologylllumina sequencingmicrobial functional diversity040103 agronomy & agriculture0401 agriculture forestry and fisheriesAlpha diversityActa Oecologica-International Journal of Ecology
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Characterization of a proton pump from Acer pseudoplatanus cell microsomes

1985

Abstract An Acer pseudoplatanus cell microsomal fraction was enriched in ATPase by sedimentation through a sucrose cushion and treatment with Triton X-100. This activity, which reached 0.9 μmol P i min −1 mg −1 protein, was specific for ATP, slightly stimulated by K + , inhibited by orthovanadate and diethylstilbestrol, insensitive to oligomycin and azide, and had a K m - value of 0.51 mM for MgATP. ATP-dependent proton translocation was demonstrated by the ΔpH probe acridine orange. This activity had a optimum at pH 6.5, was substrate specific for ATP, and was strongly dependent on K + . Preparations of plasma membrane ATPase from A. pseudoplatanus cell culture thus posses biochemical prop…

0106 biological sciencesOligomycinATPaseDiaphragm pumpPlant ScienceBiology01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants genetics03 medical and health scienceschemistry.chemical_compound[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsProton transportGenetics030304 developmental biologychemistry.chemical_classification0303 health sciencesAcridine orangeERABLE FAUX PLATANEGeneral MedicinePOMPE PROTONAcer pseudoplatanusbiology.organism_classificationEnzymeBiochemistrychemistrybiology.proteinMicrosomeAgronomy and Crop Science010606 plant biology & botanyPlant Science
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Kinetic studies on protoporphyrinogen oxidase inhibition by diphenyl ether herbicides

1991

Diphenyl ethers (DPEs) and related herbicides are powerful inhibitors of protoporphyrinogen oxidase, an enzyme involved in the biosynthesis of haems and chlorophylls. The inhibition kinetics of protoporphyrinogen oxidase of various origins by four DPEs, (methyl)-5-[2-chloro-4-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid (acifluorfen and its methyl ester, acifluorfen-methyl), methyl-5-[2-chloro-4-(trifluoromethyl) phenoxy]-2-chlorobenzoate (LS 820340) and methyl-5-[2-chloro-5-(trifluoromethyl)phenoxy]-2-nitrobenzoic acid (RH 5348), were studied. The inhibitions of the enzymes from maize (Zea mays) mitochondrial and etiochloroplastic membranes and mouse liver mitochondrial membranes were com…

0106 biological sciencesOxidoreductases Acting on CH-CH Group DonorsStereochemistry[SDV]Life Sciences [q-bio]Carboxylic acidMitochondria LiverEtherSaccharomyces cerevisiaeAcifluorfen01 natural sciencesBiochemistryMitochondrial ProteinsMiceStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundMALHERBOLOGIEPhenolsAnimalsProtoporphyrinogen OxidaseMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classification0303 health sciencesTrifluoromethylFlavoproteinsHerbicidesDiphenyl etherIntracellular MembranesCell BiologyPlantsMitochondriaProtoporphyrinogen IX[SDV] Life Sciences [q-bio]KineticsEnzymechemistryProtoporphyrinogen oxidaseOxidoreductasesEthersResearch Article010606 plant biology & botanyBiochemical Journal
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Characterization of (3H) acifluorfen binding to purified pea etioplasts, and evidence that protoporphyrinogen oxidase specifically binds acifluorfen

1992

It is now generally accepted that protoporphyrinogen oxidase is the target-enzyme for diphenylether-type herbicides. Recent studies [Camadro, J-M., Matringe, M., Scalla, R. & Labbe, P. (1991) Biochem. J. 277, 17–21] have revealed that in maize, diphenyl ethers competitively inhibit protoporphyrinogen oxidase with respect to its substrate, protoporphyrinogen IX. In this study, we show that, in purified pea etioplast, [3H]acifluorfen specifically binds to a single class of high-affinity binding sites with an apparent dissociation constant of 6.2 ± 1.3 nM and a maximum density of 29 ± 5 nmol/g protein. [3H]Acifluorfen binding reaches equilibrium in about 1 min at 30°C. Half dissociation occurs…

0106 biological sciencesOxidoreductases Acting on CH-CH Group DonorsStereochemistry[SDV]Life Sciences [q-bio]PhthalimidesAcifluorfen01 natural sciencesBiochemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundMALHERBOLOGIEEtioplastProtoporphyrinogen OxidaseBinding siteComputingMilieux_MISCELLANEOUS030304 developmental biologychemistry.chemical_classificationOrganelles0303 health sciencesOxidase testBinding SitesPlants MedicinalProtoporphyrin IXMolecular StructureBIOCHIMIEHerbicidesFabaceaeProtoporphyrinogen IX[SDV] Life Sciences [q-bio]KineticsEnzymechemistryBiochemistryNitrobenzoatesProtoporphyrinogen oxidaseOxidoreductases010606 plant biology & botany
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