Search results for "Bombykol"

showing 4 items of 4 documents

Courtship, Mating, and Sex Pheromones in the Mealworm Beetle (Tenebrio molitor)

2003

Publisher Summary This chapter focuses on courtship and mating in a coleopteran, the yellow mealworm beetle (Tenebrio molitor), observation and description of the behavior of (relatively) undisturbed animals, and the response of male Tenebrio molitor to the female sex attractant pheromone. Pheromones used in communication between members of the opposite sex in a mating context are collectively termed sex pheromones. In many insect species, detection of a sex pheromone is often sufficient to initiate the species-typical courtship and mating behaviors, although the release of these behaviors can be modified by visual, tactile, acoustic, or other types of stimuli. For example, upon detecting a…

MealwormCommunicationbusiness.industrymedia_common.quotation_subjectZoologyContext (language use)InsectBiologybiology.organism_classificationBombykolCourtshipchemistry.chemical_compoundchemistrySex pheromonePheromoneMatingbusinessmedia_common
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Conformational Change in the Pheromone-binding Protein fromBombyx mori Induced by pH and by Interaction with Membranes

1999

The pheromone-binding protein (PBP) from Bombyx mori was expressed in Escherichia coli periplasm. It specifically bound radiolabeled bombykol, the natural pheromone for this species. It appeared as a single band both in native and SDS-polyacrylamide gel electrophoresis and was also homogeneous in most chromatographic systems. However, in ion-exchange chromatography, multiple forms sometimes appeared. Attempts to separate them revealed that they could be converted into one another. Analysis of the protein by circular dichroism and fluorescence spectroscopy demonstrated that its tertiary structure was sensitive to pH changes and that a dramatic conformational transition occurred between pH 6.…

MaleConformational changeCircular dichroismSensory Receptor CellsProtein ConformationBiochemistryBombykolchemistry.chemical_compoundEscherichia coliAnimalsDenaturation (biochemistry)Pheromone bindingCloning MolecularMolecular BiologyChemistryCircular DichroismCell BiologyHydrogen-Ion ConcentrationBombyxChromatography Ion ExchangeLigand (biochemistry)Protein tertiary structureProtein Structure TertiarySpectrometry FluorescenceBiochemistryBiophysicsInsect ProteinsIntercellular Signaling Peptides and ProteinsThermodynamicsElectrophoresis Polyacrylamide GelCarrier ProteinsPheromone binding proteinJournal of Biological Chemistry
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Identification and cloning of odorant binding proteins from the scarab beetle Phyllopertha diversa.

1999

Abstract Wehave identified, cloned, and characterized two odorant binding proteins from the pale brown chafer, Phyllopertha diversa. One of the proteins (OBP1, 116 amino acids long) showed high amino acid identity (>90%) to two previously identified PBPs from scarab beetles. The second protein (OBP2) showed limited sequence similarity to lepidopteran and dipteran OBPs, but contained only 133 amino acids. Both proteins showed the occurrence of six highly conserved cysteines; electrospray mass spectral data suggested they are all bound in three disulfide bonds. During purification, OBP2 separated into several isoforms; N-terminal amino acid sequencing and electrospray ionization mass spectrom…

Gene isoformOdorant bindingElectrospray ionization1Molecular Sequence DataBiophysicsPhyllopertha diversaReceptors Odorantelectrospray mass spectrometryBiochemistryBombykolbombykolpheromonechemistry.chemical_compoundconformational changeBombyx moriAnimalsAmino Acid SequenceCloning MolecularMolecular Biologychemistry.chemical_classificationCloningbiologySequence Homology Amino Acid3H)-quinazolinedionefungi3-dimethyl-2Cell Biologybiology.organism_classificationRecombinant ProteinsjaponilureAmino acidColeopteraMolecular WeightchemistryBiochemistryOdorantsPheromone4-(1HSequence AlignmentBiochemical and biophysical research communications
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The crystal structure of a cockroach pheromone-binding protein suggests a new ligand binding and release mechanism.

2003

Pheromone-binding proteins (PBPs) are small helical proteins found in sensorial organs, particularly in the antennae, of moth and other insect species. They were proposed to solubilize and carry the hydrophobic pheromonal compounds through the antennal lymph to receptors, participating thus in the peri-receptor events of signal transduction. The x-ray structure of Bombyx mori PBP (BmorPBP), from male antennae, revealed a six-helix fold forming a cavity that contains the pheromone bombykol. We have identified a PBP (LmaPBP) from the cockroach Leucophaea maderae in the antennae of the females, the gender attracted by pheromones in this species. Here we report the crystal structure of LmaPBP a…

Models MolecularProtein FoldingProtein ConformationMolecular Sequence DataCockroachesCrystallography X-RayLigandsBiochemistryBombykolchemistry.chemical_compoundBombyx moribiology.animalAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyFluorescent DyesCockroachbiologySequence Homology Amino AcidCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationLigand (biochemistry)BombyxButanonesTransport proteinKineticschemistryBiochemistryHelixBiophysicsPheromoneInsect ProteinsFemalePheromone binding proteinCarrier ProteinsProtein BindingThe Journal of biological chemistry
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