Ligand specificity of a high-affinity binding site for lipo-chitooligosaccharidic Nod factors in Medicago cell suspension cultures
| Autor: | Julie V. Cullimore, Andreas Niebel, Jean-Jacques Bono, Raoul Ranjeva, Natacha Mantegazza, Sophie Drouillard, Frederic Gressent, Hugues Driguez, Eric Samain, Roberto A. Geremia, Hervé Canut |
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| Přispěvatelé: | Centre de Recherches sur les Macromolécules Végétales (CERMAV), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées, Centre National de la Recherche Scientifique (CNRS), Unité mixte de recherche interactions plantes-microorganismes, Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées |
| Rok vydání: | 1999 |
| Předmět: |
0106 biological sciences
nodule Stereochemistry [SDV]Life Sciences [q-bio] Biology ligand 01 natural sciences Nod factor site de liaison 03 medical and health sciences chemistry.chemical_compound rhizobium meliloti Glucosamine développement de la plante oligosaccharide nodulation Binding site Sugar ComputingMilieux_MISCELLANEOUS 030304 developmental biology chemistry.chemical_classification 0303 health sciences Multidisciplinary Medicago flore du sol medicago varia food and beverages Fatty acid Biological Sciences Ligand (biochemistry) biology.organism_classification Reducing sugar Biochemistry chemistry récepteur 010606 plant biology & botany |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America 8 (96), 4704-4709. (1999) 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, 1999, pp.4704-4709 Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 1999, 96 (8), pp.4704-4709. ⟨10.1073/pnas.96.8.4704⟩ |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.96.8.4704 |
| Popis: | Rhizobial lipo-chitooligosaccharides (LCOs) are signaling molecules involved in host-range recognition for the establishment of the symbiosis with leguminous plants. The major LCO of Rhizobium meliloti , the symbiont of Medicago plants contains four or five N -acetylglucosamines, O-acetylated and N-acylated with a C16:2 fatty acid on the terminal nonreducing sugar and O-sulfated on the reducing sugar. In this paper, the ligand specificity of a high-affinity binding site (Nod factor binding site 2 or NFBS2), enriched in a plasma membrane-enriched fraction of Medicago cell suspension cultures, is reported. By using chemically synthesized LCOs, the role of structural elements, important for symbiotic activities, as recognition motifs for NFBS2 was determined. The results show that the substitutions on the nonreducing sugar of the LCOs (the O -acetate group, the fatty acid, and the hydroxyl group on the C 4 of the sugar) are determinants for high-affinity binding to NFBS2. In contrast, the sulfate group, which is necessary for all biological activities on Medicago , is not discriminated by NFBS2. However, the reducing sugar of the LCO seems to interact with NFBS2, because ligand binding is affected by the reduction of the free anomeric carbon and depends on the number of N -acetyl glucosamine residues. These results suggest that the recognition of the LCOs by NFBS2 is mediated by structural elements in both the lipid and oligosaccharidic moities, but not by the sulfate group. |
| Databáze: | OpenAIRE |
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