Search results for "dicarboxylic acid"

showing 10 items of 75 documents

Free Radicals Mediate Systemic Acquired Resistance

2014

Summary: Systemic acquired resistance (SAR) is a form of resistance that protects plants against a broad spectrum of secondary infections. However, exploiting SAR for the protection of agriculturally important plants warrants a thorough investigation of the mutual interrelationships among the various signals that mediate SAR. Here, we show that nitric oxide (NO) and reactive oxygen species (ROS) serve as inducers of SAR in a concentration-dependent manner. Thus, genetic mutations that either inhibit NO/ROS production or increase NO accumulation (e.g., a mutation in S-nitrosoglutathione reductase [GSNOR]) abrogate SAR. Different ROS function additively to generate the fatty-acid-derived azel…

0106 biological sciences[SDV]Life Sciences [q-bio]ArabidopsisPseudomonas syringaeReductasemedicine.disease_cause01 natural scienceschemistry.chemical_compoundcuticle formationInducerDicarboxylic Acidsskin and connective tissue diseaseslcsh:QH301-705.5chemistry.chemical_classification0303 health sciencesMutationsalicyclic-acidCell biologydefenseGlutathione ReductaseBiochemistryGlycerophosphates[SDE]Environmental Sciencesplant immunitySystemic acquired resistances-nitrosoglutathioneSecondary infectionnitric-oxidearabidopsis-thalianaBiologyNitric OxideGeneral Biochemistry Genetics and Molecular BiologyNitric oxide03 medical and health sciencesmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal Biology030304 developmental biologyReactive oxygen speciesArabidopsis Proteinsfungicell-deathbody regionschemistrylcsh:Biology (General)azelaic-acidresponsesNitric Oxide SynthaseReactive Oxygen SpeciesFunction (biology)010606 plant biology & botanynitric-oxide;plant immunity;arabidopsis-thaliana;s-nitrosoglutathione;cuticle formation;salicyclic-acid;azelaic-acid;cell-death;responses;defenseCell Reports
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Transport of C(4)-dicarboxylates in Wolinella succinogenes.

2000

ABSTRACT C 4 -dicarboxylate transport is a prerequisite for anaerobic respiration with fumarate in Wolinella succinogenes , since the substrate site of fumarate reductase is oriented towards the cytoplasmic side of the membrane. W. succinogenes was found to transport C 4 -dicarboxylates (fumarate, succinate, malate, and aspartate) across the cytoplasmic membrane by antiport and uniport mechanisms. The electrogenic uniport resulted in dicarboxylate accumulation driven by anaerobic respiration. The molar ratio of internal to external dicarboxylate concentration was up to 10 3 . The dicarboxylate antiport was either electrogenic or electroneutral. The electroneutral antiport required the prese…

Anaerobic respirationAntiporterPhysiology and MetabolismMutantMalatesBiologymedicine.disease_causeMicrobiologyCell membraneElectron TransportOxygen ConsumptionBacterial ProteinsFumaratesRespirationmedicineDicarboxylic AcidsAnaerobiosisMolecular BiologyEscherichia coliDicarboxylic Acid TransportersAspartic AcidNitratesEscherichia coli ProteinsCell MembraneSodiumMembrane ProteinsBiological TransportSuccinatesFumarate reductaseElectron transport chainWolinellamedicine.anatomical_structureBiochemistryMutagenesisCarrier ProteinsGene DeletionJournal of bacteriology
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Compounds of molybdenum(VI) with aspartic acid: A spectrophotometric and potentiometric study of the formation and interconversion equilibria in aque…

1990

Addition of Na2MoO4 to an excess of aspartic acid (AspH2) can produce any of four different complexes depending on the pH, namely [MoO3(Asp)]2−, [Mo2O5(Asp)2]2−, [Mo2O4(OH)(Asp)2]− and [Mo2O4(Asp)2]. The ranges of formation of these species with pH, the number of equivalents of acid necessary for their formation, and their stoichiometries, condensation degrees and stability constants, have been calculated by potentiometric and spectrophotometric techniques. The aspartic acid acts as a tridentate ligand in all cases.

chemistry.chemical_classificationAqueous solutionChemistryInorganic chemistryPotentiometric titrationMetals and Alloyschemistry.chemical_elementMedicinal chemistryCatalysisInorganic Chemistrychemistry.chemical_compoundDicarboxylic acidMolybdenumAspartic acidMaterials ChemistryChemical equilibriumOrganometallic chemistryTransition Metal Chemistry
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CitA (citrate) and DcuS (C4-dicarboxylate) sensor kinases in thermophilic Geobacillus kaustophilus and Geobacillus thermodenitrificans

2015

The thermophilic Geobacillus thermodenitrificans and Geobacillus kaustophilus are able to use citrate or C4-dicarboxylates like fumarate or succinate as the substrates for growth. The genomes of the sequenced Geobacillus strains (nine strains) each encoded a two-component system of the CitA family. The sensor kinase of G. thermodenitrificans (termed CitAGt) was able to replace CitA of Escherichia coli (CitAEc) in a heterologous complementation assay restoring expression of the CitAEc-dependent citC-lacZ reporter gene and anaerobic growth on citrate. Complementation was specific for citrate. The sensor kinase of G. kaustophilus (termed DcuSGk) was able to replace DcuSEc of E. coli. It respon…

0301 basic medicineMolecular Sequence Data030106 microbiologyHeterologousBacillus subtilismedicine.disease_causeMicrobiologyGeobacillusCitric Acid03 medical and health sciencesBacterial ProteinsProtein-fragment complementation assaymedicineDicarboxylic AcidsAmino Acid SequenceEscherichia colibiologyThermophileGeobacillusGene Expression Regulation Bacterialbiology.organism_classificationComplementationBiochemistryHeterologous expressionProtein KinasesSequence AlignmentMicrobiology
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The Fumarate/Succinate Antiporter DcuB of Escherichia coli Is a Bifunctional Protein with Sites for Regulation of DcuS-dependent Gene Expression

2008

DcuB of Escherichia coli catalyzes C4-dicarboxylate/succinate antiport during growth by fumarate respiration. The expression of genes of fumarate respiration, including the genes for DcuB (dcuB) and fumarate reductase (frdABCD) is transcriptionally activated by C4-dicarboxylates via the DcuS-DcuR two-component system, comprising the sensor kinase DcuS, which contains a periplasmic sensing domain for C4-dicarboxylates. Deletion or inactivation of dcuB caused constitutive expression of DcuS-regulated genes in the absence of C4-dicarboxylates. The effect was specific for DcuB and not observed after inactivation of the homologous DcuA or the more distantly related DcuC transporter. Random and s…

AntiporterMutantlac operonBiologymedicine.disease_causePeptide MappingBiochemistryAntiportersFumaratesEscherichia colimedicineMolecular BiologyEscherichia coliDerepressionDicarboxylic Acid TransportersIon TransportEscherichia coli ProteinsMutagenesisSuccinatesGene Expression Regulation BacterialCell BiologyPeriplasmic spaceFumarate reductaseDNA-Binding ProteinsSuccinate DehydrogenaseAmino Acid SubstitutionBiochemistryGene Knockdown TechniquesMutagenesis Site-DirectedProtein KinasesTranscription FactorsJournal of Biological Chemistry
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Polar Localization of a Tripartite Complex of the Two-Component System DcuS/DcuR and the Transporter DctA in Escherichia coli Depends on the Sensor K…

2014

The C4-dicarboxylate responsive sensor kinase DcuS of the DcuS/DcuR two-component system of E. coli is membrane-bound and reveals a polar localization. DcuS uses the C4-dicarboxylate transporter DctA as a co-regulator forming DctA/DcuS sensor units. Here it is shown by fluorescence microscopy with fusion proteins that DcuS has a dynamic and preferential polar localization, even at very low expression levels. Single assemblies of DcuS had high mobility in fast time lapse acquisitions, and fast recovery in FRAP experiments, excluding polar accumulation due to aggregation. DctA and DcuR fused to derivatives of the YFP protein are dispersed in the membrane or in the cytosol, respectively, when …

Yellow fluorescent proteinCardiolipinslcsh:MedicineMicrobiologyMreBMicrobial PhysiologyBacterial Physiologylcsh:ScienceCytoskeletonMicrobial MetabolismDicarboxylic Acid TransportersMultidisciplinaryEscherichia coli K12biologyBacterial GrowthEscherichia coli Proteinslcsh:RMicrobial Growth and DevelopmentBiology and Life SciencesFluorescence recovery after photobleachingBacteriologyFusion proteinTwo-component regulatory systemBacterial BiochemistryTransport proteinDNA-Binding ProteinsProtein TransportBiochemistryCytoplasmMultiprotein ComplexesBiophysicsbiology.proteinlcsh:QProtein KinasesResearch ArticleDevelopmental BiologyTranscription FactorsPLoS ONE
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ChemInform Abstract: Two-Carbon Bridge Substituted Cocaines: Enantioselective Synthesis, Attribution of the Absolute Configuration, and Biological Ac…

2010

In an effort to learn more about the general structure-activity relationships of cocaine with the aim to elucidate those structural features that might confer antagonistic properties to such analogues, we describe herein our synthetic efforts to prepare two-carbon bridge functionalized (methoxylated and hydroxylated) analogues. Our approach makes use of a modification of the classical Willstatter synthesis of cocaine: Mannich type cyclization of acetonedicarboxylic acid monomethyl ester with methylamine hydrochloride and 2-methoxysuccindialdehyde in a citrate buffer solution afforded the 6- and 7-substituted 2-carbomethoxy-3-tropinones 3a,b and 4a,b in approximate yields of 64%. Reduction o…

chemistry.chemical_compoundchemistryStereochemistryEnzymatic hydrolysisAcetonedicarboxylic acidEnantioselective synthesisAbsolute configurationBiological activityGeneral MedicineEnantiomerSodium amalgamEsteraseChemInform
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The cytoplasmic PASC domain of the sensor kinase DcuS of Escherichia coli : role in signal transduction, dimer formation, and DctA interaction

2013

The cytoplasmic PAS(C) domain of the fumarate responsive sensor kinase DcuS of Escherichia coli links the transmembrane to the kinase domain. PAS(C) is also required for interaction with the transporter DctA serving as a cosensor of DcuS. Earlier studies suggested that PAS(C) functions as a hinge and transmits the signal to the kinase. Reorganizing the PAS(C) dimer interaction and, independently, removal of DctA, converts DcuS to the constitutive ON state (active without fumarate stimulation). ON mutants were categorized with respect to these two biophysical interactions and the functional state of DcuS: type I-ON mutations grossly reorganize the homodimer, and decrease interaction with Dct…

PAS domainDicarboxylic Acid TransportersModels MolecularfumarateProtein ConformationEscherichia coli ProteinsDNA Mutational AnalysisDctAModels Biological570 Life sciencessignal transduction.Escherichia coliProtein Interaction Domains and MotifsProtein MultimerizationDcuS sensor kinaseProtein KinasesOriginal ResearchSignal Transduction570 Biowissenschaften
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Production of Dicarboxylic Acids and Flagrances by Yarrowia lipolytica

2013

Yeasts are excellent biocatalysts in the field of alkane and fatty acids transformation into dicarboxylic acids and lactones. Their ability to produce some diacids through simple, less expensive and more environment friendly routes than chemical pathways and to produce particular diacids (e.g. unsaturated ones) but also to transform natural substrates into lactones with a natural label has made them the subject of many researches. Although Candida species were often first studied, the development of genetic tools, the knowledge of the genome and some genomic and biotechnological particularities of Yarrowia lipolytica resulted to interesting developments with this species. This chapter aims …

chemistry.chemical_classificationMethyl oleatebiologyChemistryRicinoleic acidYarrowiabiology.organism_classificationYeastchemistry.chemical_compoundDicarboxylic acidAmphiphileOrganic chemistryMacrocyclic lactoneCandida sp
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Functioning of DcuC as the C 4 -Dicarboxylate Carrier during Glucose Fermentation by Escherichia coli

1999

ABSTRACT The dcuC gene of Escherichia coli encodes an alternative C 4 -dicarboxylate carrier (DcuC) with low transport activity. The expression of dcuC was investigated. dcuC was expressed only under anaerobic conditions; nitrate and fumarate caused slight repression and stimulation of expression, respectively. Anaerobic induction depended mainly on the transcriptional regulator FNR. Fumarate stimulation was independent of the fumarate response regulator DcuR. The expression of dcuC was not significantly inhibited by glucose, assigning a role to DcuC during glucose fermentation. The inactivation of dcuC increased fumarate-succinate exchange and fumarate uptake by DcuA and DcuB, suggesting a…

Physiology and MetabolismMolecular Sequence DataMutantStimulationBiologymedicine.disease_causeMicrobiologyBacterial ProteinsFumaratesConsensus SequenceEscherichia colimedicineTranscriptional regulationDicarboxylic AcidsAnaerobiosisPromoter Regions GeneticMolecular BiologyEscherichia coliPsychological repressionDicarboxylic Acid TransportersBinding SitesBase SequenceEscherichia coli ProteinsSuccinatesGene Expression Regulation BacterialKineticsResponse regulatorGlucoseBiochemistryFermentationFermentationEffluxCarrier ProteinsRibosomesJournal of Bacteriology
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