Search results for "Protein domain"

showing 10 items of 132 documents

Role of Bacillus thuringiensis Cry1A toxins domains in the binding to the ABCC2 receptor from Spodoptera exigua

2018

Abstract Cry proteins from Bacillus thuringiensis (Bt) have been used to control insect pests either as formulated sprays or as in Bt-crops. However, field-evolved resistance to Bt proteins is threatening the long-term use of Bt products. The SeABCC2 locus has been genetically linked to resistance to a Bt bioinsecticide (Xentari™) in Spodoptera exigua (a mutation producing a truncated form of the transporter lacking an ATP binding domain was found in the resistant insects). Here, we investigated the role of SeABCC2 in the mode of action of Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ca, and two Cry1A-1Ca hybrids by expressing the receptor in Sf21 and HEK293T cell lines. Cell toxicity assays showed that Sf2…

0106 biological sciences0301 basic medicineCell SurvivalBacillus thuringiensisGene ExpressionSpodopteraSpodopteraTransfection01 natural sciencesBiochemistryHemolysin ProteinsStructure-Activity Relationship03 medical and health sciencesBacterial ProteinsProtein DomainsBacillus thuringiensisExiguaSf9 CellsAnimalsHumansProtein IsoformsBinding siteReceptorMolecular BiologySf21Binding SitesBacillus thuringiensis Toxinsbiologyfungibiology.organism_classificationMultidrug Resistance-Associated Protein 2Recombinant ProteinsClone CellsEndotoxins010602 entomologyHEK293 Cells030104 developmental biologyBiochemistryCry1AcLarvaInsect ScienceMutationInsect ProteinsMultidrug Resistance-Associated ProteinsPlasmidsProtein BindingBinding domainInsect Biochemistry and Molecular Biology
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Blattella germanica displays a large arsenal of antimicrobial peptide genes

2020

Defence systems against microbial pathogens are present in most living beings. The German cockroach Blattella germanica requires these systems to adapt to unhealthy environments with abundance of pathogenic microbes, in addition to potentially control its symbiotic systems. To handle this situation, four antimicrobial gene families (defensins, termicins, drosomycins and attacins) were expanded in its genome. Remarkably, a new gene family (blattellicins) emerged recently after duplication and fast evolution of an attacin gene, which is now encoding larger proteins with the presence of a long stretch of glutamines and glutamic acids. Phylogenetic reconstruction, within Blattellinae, suggests …

0106 biological sciences0301 basic medicinePore Forming Cytotoxic ProteinsGenome InsectEvolutionary biology010603 evolutionary biology01 natural sciencesGenomeArticle03 medical and health sciencesProtein DomainsPhylogeneticsGene duplicationGene expressionGene familyAnimalsAmino Acid SequenceSymbiosisGenePhylogenyRegulation of gene expressionGeneticsGerman cockroachMultidisciplinarybiologyAntimicrobial responsesBlattellidaebiology.organism_classificationGenome evolution030104 developmental biologyGene Expression RegulationEntomology
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The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion.

2017

IM30/Vipp1 proteins are crucial for thylakoid membrane biogenesis in chloroplasts and cyanobacteria. A characteristic C-terminal extension distinguishes these proteins from the homologous bacterial PspA proteins, and this extension has been discussed to be key for the IM30/Vipp1 activity. Here we report that the extension of the Synechocystis IM30 protein is indispensable, and argue that both, the N-terminal PspA-domain as well as the C-terminal extension are needed in order for the IM30 protein to conduct its in vivo function. In vitro, we show that the PspA-domain of IM30 is vital for stability/folding and oligomer formation of IM30 as well as for IM30-triggered membrane fusion. In contra…

0106 biological sciences0301 basic medicineVesicle-associated membrane protein 8ChloroplastsLipid BilayersBiophysicsBiology01 natural sciencesBiochemistryMembrane FusionThylakoidsArticle03 medical and health sciencesBacterial ProteinsProtein DomainsIntegral membrane proteinMembranesMembrane transport proteinPeripheral membrane proteinSynechocystisLipid bilayer fusionMembrane ProteinsCell BiologyCell biology030104 developmental biologyMembrane proteinMembrane biogenesisbiology.protein010606 plant biology & botanyMembrane Fusion ActivityProtein BindingBiochimica et biophysica acta. Bioenergetics
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Isolation and characterization of a Vitis vinifera transcription factor, VvWRKY1, and its effect on responses to fungal pathogens in transgenic tobac…

2007

International audience; Pathogen attack represents a major problem for viticulture and for agriculture in general. At present, the use of phytochemicals is more and more restrictive, and therefore it is becoming essential to control disease by having a thorough knowledge of resistance mechanisms. The present work focused on the trans-regulatory proteins potentially involved in the control of the plant defence response, the WRKY proteins. A full-length cDNA, designated VvWRKY1, was isolated from a grape berry library (Vitis vinifera L. cv. Cabernet Sauvignon). It encodes a polypeptide of 151 amino acids whose structure is characteristic of group IIc WRKY proteins. VvWRKY1 gene expression in …

0106 biological sciencesGénomique et Biotechnologie des FruitsPhysiologyTransgenesalicylic acid[SDV]Life Sciences [q-bio]Amino Acid MotifsMolecular Sequence DataWRKY transcription factorPlant ScienceGenetically modified cropsBiology01 natural sciences03 medical and health scienceschemistry.chemical_compoundplant resistance to pathogensGene Expression Regulation PlantComplementary DNABotanyGene expressionTobacco[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyVitisCloning MolecularPathogen030304 developmental biologyPlant Proteins2. Zero hungerGeneticschemistry.chemical_classification0303 health sciencesBase SequenceFungifood and beveragesPlants Genetically ModifiedWRKY protein domainImmunity InnateAmino acid[SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacychemistrySalicylic acid010606 plant biology & botanyTranscription Factors
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The gypsy database (GyDB) of mobile genetic elements: release 2.0

2011

This article introduces the second release of the Gypsy Database of Mobile Genetic Elements (GyDB 2.0): a research project devoted to the evolutionary dynamics of viruses and transposable elements based on their phylogenetic classification (per lineage and protein domain). The Gypsy Database (GyDB) is a long-term project that is continuously progressing, and that owing to the high molecular diversity of mobile elements requires to be completed in several stages. GyDB 2.0 has been powered with a wiki to allow other researchers participate in the project. The current database stage and scope are long terminal repeats (LTR) retroelements and relatives. GyDB 2.0 is an update based on the analys…

0106 biological sciencesProtein domainretroelementsLineage (evolution)[SDV]Life Sciences [q-bio]Retroviridae ProteinsCaulimoviridaeEukaryote evolutioncomputer.software_genrephylogeny01 natural sciencesDatabases GeneticRefSeqPhylogenyPriority journalbase de données0303 health sciencesRetrovirusPhylogenetic treeDatabaseSequence analysisdatabases geneticArticlesClassificationChemistryGenetic lineRetroelementsGenetic databaseComputer programBiologyArticleMobile genetic element03 medical and health sciencesLong terminal repeatWeb pagephylogénieVirus proteinGeneticsLife Science[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyAccess to informationTransposon030304 developmental biologyretroelements;phylogeny;software;terminal repeat sequences;databases geneticHidden Markov modelCauliflower mosaic virusCaulimovirussoftwareRetroposonTerminal Repeat SequencesDNA structureInterspersed Repetitive Sequencesterminal repeat sequencesNonhumanRetroviridaeData analysis softwareGenetic variabilityMobile genetic elementscomputerLENGUAJES Y SISTEMAS INFORMATICOSSoftware010606 plant biology & botanyPhylogenetic nomenclaturePhylogenetic tree
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Members of the WRKY gene family are upregulated in Canary palms attacked by Red Palm Weevil

2018

The Red Palm Weevil (RPW), Rhynchophorus ferrugineus, is one of the major pests affecting several palm species all around the world. The aim of this work was to identify palm genes that are responsive to RPW infestations as a valuable diagnostic tool to detect the insect attack. We have analysed a total of 15 genes that were divided in two subsets: (1) 7 genes previously linked with RPW attacks, but not involved in biotic stress responses, and (2) 8 genes encoding members of the WRKY family, a class of transcription factors well-known to be linked with both abiotic and biotic stress responses. The analysis was conducted on 4-year-old Canary palms comparing uninfested plants and infested pla…

0106 biological sciencesmedicine.disease_cause010603 evolutionary biology01 natural sciencesRhynchophorus ferrugineuSettore AGR/07 - Genetica AgrariaInfestationBotanymedicineGene familyPhoenix canariensis Hort. ex ChabaudEcology Evolution Behavior and SystematicsAbiotic componentbiologyEcologyWeevilfungifood and beveragesWRKYBiotic stressbiology.organism_classificationPalmEcology Evolution Behavior and SystematicWRKY protein domain010602 entomologyRhynchophorusSettore AGR/11 - Entomologia Generale E ApplicataInsect SciencePalmAgronomy and Crop Science
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NMR Investigation of Structures of G-Protein Coupled Receptor Folding Intermediates

2016

Folding of G-protein coupled receptors (GPCRs) according to the two-stage model (Popot, J. L., and Engelman, D. M. (1990) Biochemistry 29, 4031-4037) is postulated to proceed in 2 steps: partitioning of the polypeptide into the membrane followed by diffusion until native contacts are formed. Herein we investigate conformational preferences of fragments of the yeast Ste2p receptor using NMR. Constructs comprising the first, the first two, and the first three transmembrane (TM) segments, as well as a construct comprising TM1-TM2 covalently linked to TM7 were examined. We observed that the isolated TM1 does not form a stable helix nor does it integrate well into the micelle. TM1 is significant…

0301 basic medicine10120 Department of ChemistryBioquímicaSaccharomyces cerevisiae Proteins1303 BiochemistryProtein ConformationStereochemistrySaccharomyces cerevisiaeBiochemistryMicelleRessonància magnètica nuclear1307 Cell BiologyG03 medical and health sciencesprotein coupled receptorGPCRProtein Domains540 Chemistry1312 Molecular BiologyAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyMicellesG protein-coupled receptorSequence Homology Amino Acid030102 biochemistry & molecular biologyChemistryProteïnes de membranaFoldingCell BiologyTransloconPeptide FragmentsTransmembrane proteinNMRFolding (chemistry)Crystallography030104 developmental biologyStructural biology10036 Medical ClinicProtein Structure and FoldingReceptors Mating FactorHelixProtein folding
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Identification and Characterization of a Single High-Affinity Fatty Acid Binding Site in Human Serum Albumin.

2017

A single high-affinity fatty acid binding site in the important human transport protein serum albumin (HSA) is identified and characterized using an NBD (7-nitrobenz-2-oxa-1,3-diazol-4-yl)-C12 fatty acid. This ligand exhibits a 1:1 binding stoichiometry in its HSA complex with high site-specificity. The complex dissociation constant is determined by titration experiments as well as radioactive equilibrium dialysis. Competition experiments with the known HSA-binding drugs warfarin and ibuprofen confirm the new binding site to be different from Sudlow-sites I and II. These binding studies are extended to other albumin binders and fatty acid derivatives. Furthermore an X-ray crystal structure …

0301 basic medicineAzolesSerum albuminIbuprofenSerum Albumin HumanMolecular Dynamics Simulation010402 general chemistryCrystallography X-Ray01 natural sciencesCatalysis03 medical and health sciencesProtein DomainsFatty acid bindingmedicineFluorescence Resonance Energy TransferHumansBinding siteBovine serum albuminNitrobenzeneschemistry.chemical_classificationBinding SitesbiologyChemistry010405 organic chemistryFatty AcidsFatty acidGeneral ChemistryGeneral MedicineLigand (biochemistry)Human serum albumin0104 chemical sciencesbody regionsDissociation constant030104 developmental biologyBiochemistryembryonic structuresbiology.proteinWarfarinmedicine.drugProtein BindingAngewandte Chemie (International ed. in English)
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Role of pulmonary surfactant protein Sp-C dimerization on membrane fragmentation: An emergent mechanism involved in lung defense and homeostasis.

2020

Surfactant protein C (SP-C) is a protein present in the pulmonary surfactant system that is involved in the biophysical properties of this lipoprotein complex, but it also has a role in lung defense and homeostasis. In this article, we propose that the link between both functions could rely on the ability of SP-C to induce fragmentation of phospholipid membranes and generate small vesicles that serve as support to present different ligands to cells in the lungs. Our results using bimolecular fluorescence complementation and tunable resistive pulse sensing setups suggest that SP-C oligomerization could be the triggering event that causes membrane budding and nanovesiculation. As shown by flu…

0301 basic medicineBiophysicsBiochemistryCell Line03 medical and health sciencesBimolecular fluorescence complementation0302 clinical medicinePulmonary surfactantProtein DomainsHumansAmino Acid SequenceFragmentation (cell biology)Unilamellar LiposomesChemistryVesicleSurfactant protein CCell BiologyMembrane buddingFlow CytometryPulmonary Surfactant-Associated Protein CEndocytosisRecombinant ProteinsCell biology030104 developmental biology030228 respiratory systemMembrane proteinStructural biologyMicroscopy FluorescencePeptidomimeticsProtein MultimerizationDimerizationBiochimica et biophysica acta. Biomembranes
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Dual Constant Domain-Fab: A novel strategy to improve half-life and potency of a Met therapeutic antibody

2016

The kinase receptor encoded by the Met oncogene is a sensible target for cancer therapy. The chimeric monovalent Fab fragment of the DN30 monoclonal antibody (MvDN30) has an odd mechanism of action, based on cell surface removal of Met via activation of specific plasma membrane proteases. However, the short half-life of the Fab, due to its low molecular weight, is a severe limitation for the deployment in therapy. This issue was addressed by increasing the Fab molecular weight above the glomerular filtration threshold through the duplication of the constant domains, in tandem (DCD-1) or reciprocally swapped (DCD-2). The two newly engineered molecules showed biochemical properties comparable…

0301 basic medicineCancer ResearchMice SCIDCancer targeted therapy0302 clinical medicineMice Inbred NODEpidermal growth factor receptorPhosphorylationbiologyChemistryImmunoglobulin Fab FragmentsAntibodies MonoclonalGeneral MedicineArticlesProto-Oncogene Proteins c-metHalf-lifeCell biologyOncology030220 oncology & carcinogenesisColonic NeoplasmsMetMolecular MedicineFemalemedicine.symptomSignal transductionAntibodySignal Transductionmedicine.drug_classColonAntibody; Cancer targeted therapy; Fab; Half-life; Met; Protein engineering; Cancer Research; Genetics; Molecular MedicineAntineoplastic AgentsMonoclonal antibody03 medical and health sciencesImmunoglobulin Fab FragmentsProtein DomainsCell Line TumormedicineGeneticsAnimalsHumansFabAntibodyCell growthMolecular biology030104 developmental biologyHEK293 CellsMechanism of actionHepatocyte Growth Factor ReceptorA549 Cellsbiology.proteinProtein engineering
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