Ligand-binding properties of a juvenile hormone receptor, Methoprene-tolerant
| Autor: | Jan Rynes, Marek Jindra, Keiko Takaki, Thomas Iwema, Jean-Philippe Charles, V. Chandana Epa |
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| Přispěvatelé: | Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA), 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), Groupe de Recherche en Immunopathologies et maladies infectueuses (GRI), Université de La Réunion (UR)-Centre hospitalier Félix-Guyon [Saint-Denis, La Réunion], Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Commonwealth Scientific and Industrial Research Organisation [Canberra] (CSIRO), Biology Center, Academy of Sciences of the Czech Republic, Czech Academy of Sciences [Prague] (ASCR), University of Sud Bohemia, European Project: 276569,EC:FP7:PEOPLE,FP7-PEOPLE-2010-IOF,JHRECEPTOR(2012), Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Biology Centre of the Czech Academy of Sciences (BIOLOGY CENTRE CAS), Czech Academy of Sciences [Prague] (CAS), We thank Dr. Bruce Hammock for 3-octylthio-1,1,1-trifluoro-2-propanone (OTFP), Dr. Michel Narce for access to the radioactive facility, Francois Bonneton and Franck Borel for helpful discussions, and Jordan Ward for reading the manuscript. This work was supported by Academy of Sciences Grant 500960906 and Ministry of Education of the Czech Republic Grant 6007665801 and was partly carried out during a pre-secondment phase of Marie Curie Fellowship Award 276569 (to M.J.). This work was also supported by Czech Science Foundation Projects 204/09/H058 (to J.R.) and 204/07/1032 (to K.T.)., Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular 0106 biological sciences MESH: Signal Transduction beetle tribolium-castaneum MESH: Sequence Analysis DNA family Pyridines MESH: Drosophila domain MESH: Base Sequence Ligands 01 natural sciences chemistry.chemical_compound PAS domain MESH: Basic Helix-Loop-Helix Transcription Factors Basic Helix-Loop-Helix Transcription Factors MESH: Ligands Drosophila Proteins MESH: Animals Receptor transcription factor 0303 health sciences Tribolium drosophila-melanogaster Multidisciplinary [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] MESH: Real-Time Polymerase Chain Reaction structure modeling MESH: Transcription Factors Biological Sciences Cell biology [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] Hormone receptor MESH: Sesquiterpenes RNA Interference Drosophila Signal transduction Dimerization Sesquiterpenes MESH: Models Molecular Signal Transduction regulators MESH: Mutation MESH: Drosophila Proteins Molecular Sequence Data Protein domain MESH: RNA Interference Methoprene insecticide action Biology Real-Time Polymerase Chain Reaction 03 medical and health sciences expression Animals Immunoprecipitation Transcription factor 030304 developmental biology MESH: Molecular Sequence Data Base Sequence metamorphosis MESH: Immunoprecipitation MESH: Pyridines Sequence Analysis DNA Molecular biology proteins 010602 entomology MESH: Methoprene chemistry MESH: Dimerization Mutation Juvenile hormone molecular actions Transcription Factors |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2011, 108, pp.21128-21133. ⟨10.1073/pnas.1116123109⟩ Proceedings of the National Academy of Sciences of the United States of America, 2011, 108 (52), pp.21128-21133. ⟨10.1073/pnas.1116123109⟩ Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2011, 108 (52), pp.21128-21133. ⟨10.1073/pnas.1116123109⟩ |
| ISSN: | 0027-8424 1091-6490 |
| DOI: | 10.1073/pnas.1116123109⟩ |
| Popis: | http://www.pnas.org/; International audience; Juvenile hormone (JH) is a sesquiterpenoid of vital importance for insect development, yet the molecular basis of JH signaling remains obscure, mainly because a bona fide JH receptor has not been identified. Mounting evidence points to the basic helix-loop-helix (bHLH)/Per-Arnt-Sim (PAS) domain protein Methoprene-tolerant (Met) as the best JH receptor candidate. However, details of how Met transduces the hormonal signal are missing. Here, we demonstrate that Met specifically binds JH III and its biologically active mimics, methoprene and pyriproxyfen, through its C-terminal PAS domain. Substitution of individual amino acids, predicted to form a ligand-binding pocket, with residues possessing bulkier side chains reduces JH III binding likely because of steric hindrance. Although a mutation that abolishes JH III binding does not affect a Met-Met complex that forms in the absence of methoprene, it prevents both the ligand-dependent dissociation of the Met-Met dimer and the ligand-dependent interaction of Met with its partner bHLH-PAS protein Taiman. These results show that Met can sense the JH signal through direct, specific binding, thus establishing a unique class of intracellular hormone receptors. |
| Databáze: | OpenAIRE |
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