The Drosophila odorant-binding protein 28a is involved in the detection of the floral odour ß-ionone
| Autor: | Martine Maïbèche, Daniel Gonzalez, Fabrice Neiers, Nicolas Poirier, Stéphane Fraichard, Thomas Chertemps, Guillaume Gotthard, Loïc Briand, Karen Rihani, Jean-François Ferveur |
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| Přispěvatelé: | Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), European Synchrotron Radiation Facility (ESRF), Institut d'écologie et des sciences de l'environnement de Paris (iEES Paris), Institut National de la Recherche Agronomique (INRA)-Sorbonne Université (SU)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), The Institut National de la Recherche Agronomique, the Centre National de la Recherche Scientifique, the Université de Bourgogne-Franche Comté, the Bourgogne-Franche Comté Regional Council (PARI 2010–2011–2012, AGRALE1 Project)., Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS), Institut d'écologie et des sciences de l'environnement de Paris (IEES (UMR_7618 / UMR_D_242 / UMR_A_1392 / UM_113) ) |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Protein Conformation
[SDV]Life Sciences [q-bio] Mutant Olfaction [SDV.BC]Life Sciences [q-bio]/Cellular Biology Ligands Receptors Odorant law.invention 03 medical and health sciences Cellular and Molecular Neuroscience pheromone law Animals Drosophila Proteins [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Receptor Molecular Biology odorant Binding selectivity Pharmacology 0303 health sciences odorant-protein-binding biology Chemistry Ligand binding assay Drosophila Melanogaster 030302 biochemistry & molecular biology fungi Cell Biology assay biology.organism_classification Smell Biochemistry Recombinant DNA Odorant-binding protein biology.protein Intercellular Signaling Peptides and Proteins Molecular Medicine insect Drosophila melanogaster Norisoprenoids Gene Deletion olfaction |
| Zdroj: | Cellular and Molecular Life Sciences Cellular and Molecular Life Sciences, Springer Verlag, 2020, 77 (13), pp.2565-2577. ⟨10.1007/s00018-019-03300-4⟩ Cellular and Molecular Life Sciences, Springer Verlag, In press, ⟨10.1007/s00018-019-03300-4⟩ |
| ISSN: | 1420-682X 1420-9071 |
| DOI: | 10.1007/s00018-019-03300-4⟩ |
| Popis: | International audience; Odorant-binding proteins (OBPs) are small soluble proteins that are thought to transport hydrophobic odorants across the aqueous sensillar lymph to olfactory receptors. A recent study revealed that OBP28a, one of the most abundant Drosophila OBPs, is not required for odorant transport, but acts in buffering rapid odour variation in the odorant environment. To further unravel and decipher its functional role, we expressed recombinant OBP28a and characterized its binding specificity. Using a fluorescent binding assay, we found that OBP28a binds a restricted number of floral-like chemicals, including ß-ionone, with an affinity in the micromolar range. We solved the X-ray crystal structure of OBP28a, which showed extensive conformation changes upon ligand binding. Mutant flies genetically deleted for the OBP28a gene showed altered responses to ß-ionone at a given concentration range, supporting its essential role in the detection of specific compounds present in the natural environment of the fly. |
| Databáze: | OpenAIRE |
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