Search results for "Molecular sequence"

showing 10 items of 1972 documents

A new self-compatibility haplotype in the sweet cherry 'Kronio', S5' attributable to a pollen-part mutation in the SFB gene

2008

‘Kronio’ is a Sicilian cultivar of sweet cherry (Prunus avium), nominally with the incompatibility genotype S 5 S 6 , that is reported to be naturally self-compatible. In this work the cause of its self-compatibility was investigated. Test selfing confirmed self-compatibility and provided embryos for analysis; PCR with consensus primers designed to amplify S-RNase and SFB alleles showed that the embryos were of two types, S 5 S 5 and S 5 S 6 , indicating that S 6 pollen failed, but S 5 succeeded, perhaps because of a mutation in the pollen or stylar component. Stylar RNase analysis indicated active S-RNases for both S 5 and S 6 . The S-RNase alleles were cloned and sequenced; and sequences …

PhysiologyMolecular Sequence DataPlant ScienceFlowersBiologyPolymerase Chain ReactionPrunusRibonucleasesChromosome SegregationGenotypeAmino Acid SequencePollinationGeneAllelesCrosses GeneticGeneticsF-Box ProteinsHaplotypeIntronfood and beveragesSelfingSequence Analysis DNAHaplotypesSeedlingsMutationMicrosatellitePrunusPloidy
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Thermostability of Two Cyanobacterial GrpE Thermosensors

2011

GrpE proteins act as co-chaperones for DnaK heat-shock proteins. The dimeric protein unfolds under heat stress conditions, which results in impaired interaction with a DnaK protein. Since interaction of GrpE with DnaK is crucial for the DnaK chaperone activity, GrpE proteins act as a thermosensor in bacteria. Here we have analyzed the thermostability and function of two GrpE homologs of the mesophilic cyanobacterium Synechocystis sp. PCC 6803 and of the thermophilic cyanobacterium Thermosynechococcus elongatus BP1. While in Synechocystis an N-terminal helix pair of the GrpE dimer appears to be the thermosensing domain and mainly mediates GrpE dimerization, the C-terminal four-helix bundle i…

PhysiologyMolecular Sequence DataProtein domainPlant SciencePlasma protein bindingCyanobacteriaProtein structureBacterial ProteinsHeat shock proteinEscherichia coliAmino Acid SequencePeptide sequenceHeat-Shock ProteinsThermostabilitySequence Homology Amino AcidbiologyProtein StabilityChemistryCircular DichroismGenetic Complementation TestSynechocystisSynechocystisTemperatureCell BiologyGeneral Medicinebiology.organism_classificationProtein Structure TertiaryCross-Linking ReagentsChaperone (protein)Biophysicsbiology.proteinbacteriaProtein MultimerizationProtein BindingPlant and Cell Physiology
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The Arabidopsis COPT6 Transport Protein Functions in Copper Distribution Under Copper-Deficient Conditions

2013

Copper (Cu), an essential redox active cofactor, participates in fundamental biological processes, but it becomes highly cytotoxic when present in excess. Therefore, living organisms have established suitable mechanisms to balance cellular and systemic Cu levels. An important strategy to maintain Cu homeostasis consists of regulating uptake and mobilization via the conserved family of CTR/COPT Cu transport proteins. In the model plant Arabidopsis thaliana, COPT1 protein mediates root Cu acquisition, whereas COPT5 protein functions in Cu mobilization from intracellular storage organelles. The function of these transporters becomes critical when environmental Cu bioavailability diminishes. Ho…

PhysiologyMolecular Sequence DataSaccharomyces cerevisiaeMutantArabidopsisSaccharomyces cerevisiaePlant SciencePlant RootsCofactorCell membraneGene Expression Regulation PlantArabidopsisOrganellemedicineHomeostasisAmino Acid SequenceSLC31 ProteinsbiologyArabidopsis ProteinsMembrane transport proteinCell MembraneGenetic Complementation TestMembrane Transport ProteinsBiological TransportCell BiologyGeneral MedicinePlants Genetically Modifiedbiology.organism_classificationUp-RegulationTransport proteinCell biologyPlant LeavesMutagenesis Insertionalmedicine.anatomical_structureBiochemistrySeedsbiology.proteinPlant Vascular BundleSequence AlignmentCopperPlant ShootsPlant and Cell Physiology
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Functional characterization of the plastidial 3-phosphoglycerate dehydrogenase family in Arabidopsis.

2013

This work contributes to unraveling the role of the phosphorylated pathway of serine (Ser) biosynthesis in Arabidopsis (Arabidopsis thaliana) by functionally characterizing genes coding for the first enzyme of this pathway, 3-phosphoglycerate dehydrogenase (PGDH). We identified two Arabidopsis plastid-localized PGDH genes (3-PGDH and EMBRYO SAC DEVELOPMENT ARREST9 [EDA9]) with a high percentage of amino acid identity with a previously identified PGDH. All three genes displayed a different expression pattern indicating that they are not functionally redundant. pgdh and 3-pgdh mutants presented no drastic visual phenotypes, but eda9 displayed delayed embryo development, leading to aborted emb…

PhysiologyMutantMolecular Sequence DataArabidopsisPlant SciencePlant RootsGene Expression Regulation EnzymologicSerineBiochemistry and MetabolismGene Expression Regulation PlantComplementary DNAArabidopsisGeneticsSerineArabidopsis thalianaMetabolomicsAmino Acid SequencePlastidsPhosphorylationGenePhosphoglycerate DehydrogenasePhylogenyTapetumMicroscopy ConfocalbiologySequence Homology Amino AcidArabidopsis ProteinsReverse Transcriptase Polymerase Chain ReactionGenetic Complementation Testfood and beveragesPlant Components Aerialbiology.organism_classificationPlants Genetically ModifiedPhenotypeIsoenzymesBiochemistryMultigene FamilyMutationSeedsPollenPlant physiology
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Identification of the Weevil immune genes and their expression in the bacteriome tissue

2008

Abstract Background Persistent infections with mutualistic intracellular bacteria (endosymbionts) are well represented in insects and are considered to be a driving force in evolution. However, while pathogenic relationships have been well studied over the last decades very little is known about the recognition of the endosymbionts by the host immune system and the mechanism that limits their infection to the bacteria-bearing host tissue (the bacteriome). Results To study bacteriome immune specificity, we first identified immune-relevant genes of the weevil Sitophilus zeamais by using suppressive subtractive hybridization (SSH) and then analyzed their full-length coding sequences obtained b…

PhysiologyPlant Scienceprotéines et peptides de signalisation intracellulaireStructural BiologyGene expressionlcsh:QH301-705.5Genetics0303 health sciencesAgricultural and Biological Sciences(all)EndosymbiosisReverse Transcriptase Polymerase Chain ReactionMicrobiology and ParasitologyIntracellular Signaling Peptides and ProteinsMicrobiologie et ParasitologielarveLarva1-1-1 Article périodique à comité de lectureInsect ProteinsGeneral Agricultural and Biological SciencesResearch ArticleBiotechnologyexpression géniquecharanconMolecular Sequence DatamuramidaseBiologyGeneral Biochemistry Genetics and Molecular BiologyMicrobiology03 medical and health sciencesAposymbioticcurculionidaeImmune systemEscherichia coliAnimalsGeneEcology Evolution Behavior and SystematicsAlphaproteobacteria030304 developmental biologyBiochemistry Genetics and Molecular Biology(all)030306 microbiologyTOLLIPIntracellular parasitefungiBacteriomeCell Biologybiochemical phenomena metabolism and nutritionGene Expression Regulationlcsh:Biology (General)WeevilsbacteriaCarrier ProteinsAntimicrobial Cationic Peptides[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/SymbiosisDevelopmental BiologyBMC Biology
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Molecular characterization and evolution of the protein phosphatase 2A B' regulatory subunit family in plants.

2002

Abstract Type 2A serine/threonine protein phosphatases (PP2A) are important components in the reversible protein phosphorylation events in plants and other organisms. PP2A proteins are oligomeric complexes constituted by a catalytic subunit and several regulatory subunits that modulate the activity of these phosphatases. The analysis of the complete genome of Arabidopsis allowed us to characterize four novel genes, AtB′ε, AtB′ζ,AtB′η, and AtB′θ, belonging to the PP2A B′ regulatory subunit family. Because four genes of this type had been described previously, this family is composed of eight members. Reverse transcriptase-polymerase chain reaction experiments showed thatAtB′ε mRNAs are prese…

PhysiologyProtein subunitMolecular Sequence DataArabidopsisPlant ScienceGene Expression Regulation EnzymologicEvolution MolecularGene Expression Regulation PlantArabidopsisGeneticsPhosphoprotein PhosphatasesArabidopsis thalianaProtein phosphorylationAmino Acid SequenceProtein Phosphatase 2GenePeptide sequencePhylogenyGenomic organizationGeneticsExpressed Sequence TagsbiologySequence Homology Amino AcidOryzaProtein phosphatase 2Plantsbiology.organism_classificationIsoenzymesBiochemistryMultigene FamilyResearch ArticlePlant physiology
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Similarities and singularities of three DnaK proteins from the cyanobacterium Synechocystis sp. PCC 6803.

2010

In the genome of completely sequenced mesophilic cyanobacterium Synechocystis sp. PCC 6803 three DnaK proteins are encoded, which share a high degree of sequence identity in their N-terminal ATPase region as well as in the adjacent peptide-binding domain. However, as typical for DnaK proteins, the C-termini of the three Synechocystis proteins are highly diverse. To study the functions of the three Synechocystis DnaK proteins in more detail, we have analyzed the abundance of the individual proteins in Synechocystis cells as well as dnaK expression under various stress conditions. The presented results show that all three Synechocystis DnaK proteins interact with the same GrpE nucleotide exch…

Physiologygenetic processesAmino Acid MotifsMolecular Sequence DataSequence alignmentPlant SciencePlasma protein bindingBiologymedicine.disease_causeMicrobiologyConserved sequenceNucleotide exchange factorBacterial ProteinsStress PhysiologicalmedicineHSP70 Heat-Shock ProteinsAmino Acid SequencePeptide sequenceConserved SequenceHeat-Shock ProteinsMutationSynechocystisSynechocystisCell BiologyGeneral MedicineGene Expression Regulation Bacterialbiology.organism_classificationBiochemistrybiological sciencesMutationbacteriaSequence AlignmentFunction (biology)Protein BindingPlantcell physiology
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Physostigmine and Neuromuscular Transmission

1993

Single channel studies carried out in cultured rat myoballs and cultured hippocampal neurons, and ion flux studies performed on Torpedo electrocyte membrane vesicles, showed that physostigmine (Phy), a well-established acetylcholinesterase inhibitor, interacts directly with nicotinic acetylcholine receptors (nAChR). Low concentrations (0.1 microM) of Phy activate the receptor integral channel, whereas higher concentrations blocked the channel in its opened state. In contrast to channel activation by acetylcholine (ACh) and classical cholinergic agonists, however, Phy was capable of activating the nAChR channel even when the ACh binding sites were blocked by competitive antagonists, such as …

PhysostigmineMolecular Sequence DataNeuromuscular JunctionNeuromuscular transmissionIn Vitro TechniquesReceptors NicotinicTorpedoHippocampusSynaptic TransmissionGeneral Biochemistry Genetics and Molecular BiologyNeuromuscular junctionHistory and Philosophy of SciencemedicineAnimalsAmino Acid SequencePatch clampBinding siteCells CulturedAcetylcholine receptorBinding SitesChemistryGeneral NeuroscienceAcetylcholineRatsQuaternary Ammonium CompoundsNicotinic agonistmedicine.anatomical_structureBiophysicsCholinergicIon Channel GatingNeuroscienceAcetylcholinemedicine.drugAnnals of the New York Academy of Sciences
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Photoaffinity labeling of Torpedo acetylcholine receptor by physostigmine.

1993

The plant alkaloid physostigmine, an established anti-cholinesterase agent of the carbamate type, has recently been shown to bind to the nicotinic acetylcholine receptor from Torpedo marmorata electrocytes [Okonjo, K. O., Kuhlmann, J.Maelicke, A. (1991) Eur. J. Biochem. 200, 671-677]. Pharmacological studies of physostigmine-induced ion flux into nicotinic-acetylcholine-receptor-rich membrane vesicles, indicated distinct binding sites for physostigmine and acetylcholine. As shown in this study by photoaffinity labeling with [phenyl-(n)-3H](-)physostigmine, the physostigmine-binding site is located within the same subunit (alpha polypeptide) of the receptor as the acetylcholine-binding site.…

PhysostigmineStereochemistryPhotochemistryUltraviolet RaysPhysostigmineMolecular Sequence DataReceptors NicotinicTorpedoTritiumBiochemistrylaw.inventionlawmedicineAnimalsAmino Acid SequenceAcetylcholine receptorBinding SitesPhotoaffinity labelingChemistryAffinity LabelsBungarotoxinLigand (biochemistry)Nicotinic acetylcholine receptorBiochemistryTorpedoAcetylcholinemedicine.drugEuropean journal of biochemistry
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Are elicitins cryptograms in plant-oomycete communications?

1999

Stimulation of plant natural defenses is an important challenge in phytoprotection prospects. In that context, elicitins, which are small proteins secreted by Phytophthora and Pythium species, have been shown to induce a hypersensitive-like reaction in tobacco plants. Moreover, these plants become resistant to their pathogens, and thus this interaction constitutes an excellent model to investigate the signaling pathways leading to plant resistance. However, most plants are not reactive to elicitins, although they possess the functional signaling pathways involved in tobacco responses to elicitin. The understanding of factors involved in this reactivity is needed to develop agronomic applica…

Phytophthora0106 biological sciences[SDV]Life Sciences [q-bio]Molecular Sequence DataMutagenesis (molecular biology technique)Context (language use)01 natural sciencesHost-Parasite InteractionsEvolution MolecularFungal Proteins03 medical and health sciencesCellular and Molecular NeuroscienceErgosterolGene Expression Regulation FungalTobaccoPlant defense against herbivoryAmino Acid SequenceMolecular BiologyPhylogenyComputingMilieux_MISCELLANEOUSPlant Diseases030304 developmental biologyPharmacologyOomycete0303 health sciencesBase SequencebiologyAlgal Proteinsfungifood and beveragesElicitinCell Biologybiology.organism_classification[SDV] Life Sciences [q-bio]Plants ToxicOomycetesBiochemistryMolecular MedicinePhytophthoraSequence AlignmentPlant lipid transfer proteinsFunction (biology)BiotechnologySignal Transduction010606 plant biology & botany
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