Search results for "CERCOSPORA BETICOLA"

showing 8 items of 8 documents

Cercospora leaf spot of sugar beet (Cercospora beticola Sacc.) Part I. Biology and occurrence

2019

Cercospora beticola Sacc. jest najgroźniejszym patogenem liści buraka cukrowego we wszystkich rejonach uprawy tej rośliny. W niniejszym opracowaniu zebrano najważniejszą wiedzę dotyczącą pozycji systematycznej, biologii, morfologii grzyba oraz jego żywicieli. Opisano warunki, w których dochodzi do infekcji roślin gospodarza oraz wpływ warunków atmosferycznych na rozwój choroby na roślinach. Podano podstawowe informacje na temat rozprzestrzeniania się oraz zimowania C. beticola w warunkach naturalnych. Opisano wpływ na rośliny gospodarza oraz powodowane straty w plonie korzeni i cukru. Całość zagadnienia omówiono w oparciu o polską i światową szeroką bazę literaturową.

Cercospora beticolawarunki pogodowe infekcjiCercospora beticola; biology; morphology and taxonomy of fungus; infection weather condition; disease harmfulness;morfologia i taksonomia grzybaszkodliwość chorobybiologiaProgress in Plant Protection/Postępy w Ochronie Roślin
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Cercospora beticola toxins. Part XVII. The role of the beticolin/Mg2+ complexes in their biological activity Study of plasma membrane H+-ATPase, vacu…

1996

Beticolin-1 and beticolin-2, yellow toxins produced by the phytopathogenic fungus Cercospora beticola, inhibit the plasma membrane H(+)-ATPase. Firstly, since beticolins are able to form complexes with Mg2+, the role of the beticolin/Mg2+ complexes in the inhibition of the plasma membrane proton pump has been investigated. Calculations indicate that beticolins could exist under several forms, in the H(+)-ATPase assay mixture, both free or complexed with Mg2+. However, the percentage inhibition of the H(+)-ATPase activity is correlated to the concentration of one single form of beticolin, the dimeric neutral complex Mg2H2B2, which appears to be the active form involved in the H(+)-ATPase inh…

Pyrophosphatase H+-StereochemistryATPaseAcid PhosphatasePhosphataseBiophysicsBiological Transport ActiveHeterocyclic Compounds 4 or More RingsZea maysBiochemistryMagnesium ion complexH+- PyrophosphataseMagnesiumEnzyme InhibitorsPyrophosphatasesInhibitionchemistry.chemical_classificationATPase H+-biologyChemistryVacuolar hCell MembraneSubstrate (chemistry)Biological activityCell BiologyMycotoxinsAlkaline PhosphataseCercospora beticolabiology.organism_classificationInorganic PyrophosphataseProton-Translocating ATPasesBeticolinMembraneEnzymeBiochemistryVacuolesbiology.proteinH+- ATPaseBiochimica et Biophysica Acta (BBA) - Biomembranes
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Cercospora beticola toxins. Use of fluorescent cyanine dye to study their effects on tobacco cell suspensions

1996

Abstract The fluorescent dye 3,3′-diethylthiadicarbocyanine iodide [diS-C 2 -(5)] was used to observe plasmalemma transmembrane potential variations of tobacco cells treated with uncoupler (FCCP), respiratory inhibitors (azide and cyanide), and H + -ATPase inhibitors (DCCD and a carbanilate derivative). These chemicals induced an increase in fluorescence, indicating a dissipation of the transmembrane potential. The [diS-C 2 -(5)] was also used to study the effects of two Cercospora beticola toxins on tobacco cells. Changes in fluorescence of [diS-C 2 -(5)] suggested that these two toxins caused a dissipation of the transmembrane potential with a different magnitude whereas kinetics of their…

0106 biological sciencesCyanideATPasePlant ScienceHorticultureBiology01 natural sciencesBiochemistry03 medical and health scienceschemistry.chemical_compoundCyanineMolecular Biology[SDV.BV.PEP] Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacyComputingMilieux_MISCELLANEOUS030304 developmental biologyMembrane potential0303 health sciencesGeneral MedicineCercospora beticolabiology.organism_classificationFluorescence[SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacyMembranechemistryBiochemistrybiology.proteinAzide010606 plant biology & botany
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Beticolins: chemistry and biological activities

2010

Part II: Biology of Cercospora beticola C)Toxins of Cercospora

[SDV] Life Sciences [q-bio][SDE] Environmental SciencesMYCOLOGY[SDV]Life Sciences [q-bio][SDE]Environmental SciencesCERCOSPORA BETICOLASUGAR BEETDISEASEPLANT PATHOLGY
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Cercospora beticola toxins. IX. Relationship between structure of beticolins, inhibition of plasma membrane H+ -ATPase and partition in lipid membran…

1996

Beticolins are yellow toxins produced by the fungus Cercospora beticola. The effect of one of them, beticolin-1, has been investigated on corn root plasma membrane H + -ATPase (EC 3.6.1.35) at different purification levels (plasma membrane fraction. partially, or highly purified enzyme). The results obtained demonstrated that (1) the purified proton pump was inhibited directly by low amounts of the toxin (I 50 =1.62 ± 0.18 μM), (2) the biological effects of beticolin-1 were similar to those of CBT (Cercospora beticola toxin). Furthermore, it was established that the efficiency of the different beticolins was clearly related to their ability to interact with the lipid bilayers, determined by…

0106 biological sciencesSTRUCTUREPhysiologyATPasePlant Science010402 general chemistrymedicine.disease_cause01 natural sciencesProton transportGeneticsmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyLipid bilayerComputingMilieux_MISCELLANEOUSchemistry.chemical_classificationLiposomeChromatographybiologyChemistryToxinCell BiologyGeneral MedicineCercospora beticolabiology.organism_classification0104 chemical sciencesMembraneEnzymeBiochemistrybiology.protein010606 plant biology & botany
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Cercospora beticola Toxin Inhibits Vanadate-Sensitive H+ Transport in Corn Root Membrane Vesicles

1988

The effect of Cercospora beticola toxin on the transport of protons by vanadate-sensitive ATPase was studied with corn (Zea mays) root microsomal vesicles prepared by differential centrifugation, sedimentation through a sucrose cushion, and washing with Triton X-100 plus KBr. In these preparations, addition of ATP induced intravesicular H(+)-accumulation as evidenced by a rapid quenching of the fluorescence of 9-amino-6-chloro-2-methoxy acridine. This quenching was relatively unaffected by inhibitors of mitochondrial and tonoplast-type ATPases, but was strongly reduced by inhibitors of plasma membrane H(+)-ATPase. C. beticola toxin markedly inhibited ATP dependent H(+)-transport, and this e…

0106 biological sciencesPhysiology[SDV]Life Sciences [q-bio]ATPasePlant Sciencemedicine.disease_cause01 natural sciences03 medical and health sciencesGeneticsmedicineVanadateMembranes and BioenergeticsCERCOSPORA BETICULAComputingMilieux_MISCELLANEOUS030304 developmental biologyDifferential centrifugation0303 health sciencesQuenching (fluorescence)biologyToxinVesicleMembrane transportCercospora beticolabiology.organism_classification[SDV] Life Sciences [q-bio]Biochemistrybiology.protein010606 plant biology & botanyPlant Physiology
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The yellow toxins produced by Cercospora Beticola. Part VIII : Chemical equilibrium between beticolins ; structures of minor compounds : beticolin 6 …

1994

Abstract a general chemical transformation of the “linear” beticolin skeleton (beticolin 2 and 4) into a “bent” beticolin skeleton (cebetin A and beticolin 3 respectively) is described. Beticolins 6 and 8, minor components of mycelial extract are also characterized as minor compounds resulting from these transformations.

Chemical transformationbiologyChemistryStereochemistryOrganic ChemistryDrug DiscoveryChemical equilibriumCercospora beticolabiology.organism_classificationBiochemistryTetrahedron Letters
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Magnesium ions promote assembly of channel-like structures from beticolin 0, a non-peptide fungal toxin purified from Cercospora beticola.

1998

Beticolins are toxins produced by the fungus Cercospora beticola. Using beticolin 0 (B0), we have produced a strong and Mg(2+)-dependent increase in the membrane conductance of Arabidopsis protoplasts and Xenopus oocytes. In protein-free artificial bilayers, discrete deflexions of current were observed (12 pS unitary conductance in symmetrical 100 mM KCl) in the presence of B0 (approximately 10 microM) and in the presence of nominal Mg2+. Addition of 50 microM Mg2+ induced a macroscopic current which could be reversed to single channel current by chelating Mg2+ with EDTA. Both unitary and macroscopic currents were ohmic. The increase in conductance of biological membranes triggered by B0 is…

0106 biological sciencesCations DivalentXenopusPlant Science01 natural sciencesHeterocyclic Compounds 4 or More RingsIon ChannelsDivalentMembrane Potentials03 medical and health sciencesAscomycotaBotanyGeneticsAnimalsMagnesiumMagnesium ion030304 developmental biologychemistry.chemical_classificationMembrane potential0303 health sciencesbiologyCell MembraneConductanceBiological membraneCell BiologyMembrane transportMycotoxinsCercospora beticolabiology.organism_classificationchemistryBiophysicsOocytesMembrane channel010606 plant biology & botanyThe Plant journal : for cell and molecular biology
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