0000000000180142

AUTHOR

Eric Gomés

0000-0003-2582-1203

showing 5 related works from this author

Activation of the plant plasma membrane H+ -ATPase. Is there a direct interaction between lysophosphatidylcholine and the C-terminal part of the enzy…

1996

The antagonistic effects of the fungal toxin beticolin-1 and of L-alpha-lysophosphatidylcholine (lysoPC) were investigated on the plasma membrane H+-ATPase of the plant Arabidopsis thaliana (isoform 2) expressed in yeast, using both wild-type enzyme (AHA2) and C-terminal truncated enzyme (aha2delta92). Phosphohydrolytic activities of both enzymes were inhibited by beticolin-1, with very similar 50% inhibitory concentrations, indicating that the toxin action does not involve the C-terminal located autoinhibitory domain of the proton pump. Egg lysoPC, a compound that activates the H+-ATPase by a mechanism involving the C-terminal part of the protein, was found to be able to reverse the inhibi…

0106 biological sciencesATPaseArabidopsismedicine.disease_cause01 natural sciencesBiochemistrychemistry.chemical_compoundStructural BiologyArabidopsis thalianaComputingMilieux_MISCELLANEOUSchemistry.chemical_classification0303 health sciencesbiologyPlantsRecombinant ProteinsIsoenzymesBeticolinProton-Translocating ATPasesLysophosphatidylcholineMembraneBiochemistryPlasma membrane H+-ATPase activationGene isoformAutoinhibitory domainDetergentsBiophysicsSaccharomyces cerevisiae[SDV.BC]Life Sciences [q-bio]/Cellular BiologyHeterocyclic Compounds 4 or More RingsStructure-Activity Relationship03 medical and health sciencesGeneticsmedicine[SDV.BC] Life Sciences [q-bio]/Cellular BiologyMolecular Biology030304 developmental biologyBinding SitesToxinCell MembraneLysophosphatidylcholinesCell BiologyMycotoxinsbiology.organism_classificationYeastEnzyme Activationl-α-LysophosphatidylcholineEnzymechemistryLiposomesbiology.protein010606 plant biology & botany
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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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Modulation of the Biological Activity of a Tobacco LTP1 by Lipid Complexation

2004

Plant lipid transfer proteins (LTPs) are small, cysteine-rich proteins secreted into the extracellular space. They belong to the pathogenesis-related proteins (PR-14) family and are believed to be involved in several physiological processes including plant disease resistance, although their precise biological function is still unknown. Here, we show that a recombinant tobacco LTP1 is able to load fatty acids and jasmonic acid. This LTP1 binds to specific plasma membrane sites, previously characterized as elicitin receptors, and is shown to be involved in the activation of plant defense. The biological properties of this LTP1 were compared with those of LTP1-linolenic and LTP1-jasmonic acid…

Phytophthora0106 biological sciences[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringCyclopentanesPlasma protein bindingBiologyFatty Acid-Binding ProteinsLigands01 natural sciencesMass SpectrometryFatty acid-binding proteinCell membrane03 medical and health scienceschemistry.chemical_compoundTobacco[SDV.IDA]Life Sciences [q-bio]/Food engineeringExtracellularmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal Biology[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringOxylipinsMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesDose-Response Relationship DrugCircular DichroismJasmonic acidCell MembraneFatty AcidsElicitinBiological activityArticlesCell Biology[SDV.IDA] Life Sciences [q-bio]/Food engineeringLipid MetabolismLipidsRecombinant Proteinsmedicine.anatomical_structureBiochemistrychemistryPHYTOPHTORA PARASITICACarrier ProteinsTRANSFERT LIPIDIQUEPlant lipid transfer proteinsChromatography LiquidProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
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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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Differences in berry primary and secondary metabolisms identified by transcriptomic and metabolic profiling of two table grape color somatic variants

2019

ABSTRACTAnthocyanins are flavonoids responsible for the color of berries in skin-pigmented grapevine (Vitis vinifera L.). Due to the widely adopted vegetative propagation of this species, somatic mutations occurring in meristematic cell layers can be fixed and passed into the rest of the plant when cloned. In this study we focused on the transcriptomic and metabolic differences between two color somatic variants. Using microscopic, metabolic and mRNA profiling analyses we compared the table grape cultivar (cv.) ‘Red Globe’ (RG, with purplish berry skin) and cv. ‘Chimenti Globe’ (CG, with a contrasting reddish berry skin color). As expected, significant differences were found in the composit…

PeonidinCyanidinfungiPrimary metabolitefood and beveragesBerryBiologybiology.organism_classificationMalvidinRed Globechemistry.chemical_compoundchemistryBiochemistryPetunidinDelphinidin
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