The structure was elucidated in this paper NCBI PubMed ID:23808871 Publication DOI:10.1021/cb400369u Journal NLM ID:101282906 Publisher: Washington, DC: American Chemical Society Correspondence: Jean-Jacques.Bonotoulouse.inra.fr Institutions: INRA, Laboratoire des Interactions Plantes-Microorganismes (LIPM), Castanet-Tolosan, France, CNRS, Laboratoire des Interactions Plantes-Microorganismes (LIPM), Castanet-Tolosan, France, Université Paris-Sud and CNRS, Laboratoire de Synthèse de Biomolécules, Institut de Chimie Moléculaire et des Matériaux d’Orsay, Orsay, France, Université de Toulouse, Laboratoire de Recherche en Sciences Végétales (LRSV), Castanet-Tolosan, France, CNRS, Castanet-Tolosan, France, Plateforme de Protéomique, Toulouse, France, Centre de Recherches sur les Macromolécules Végétales, Grenoble, France, Centre de Recherche de Gif, Institut de Chimie des Substances Naturelles du CNRS, Gif-sur-Yvette,France, School of Pharmaceutical Sciences, Geneva, Switzerland
While chitooligosaccharides (COs) derived from fungal chitin are potent elicitors of defense reactions, structurally related signals produced by certain bacteria and fungi, called lipo-chitooligosaccharides (LCOs), play important roles in the establishment of symbioses with plants. Understanding how plants distinguish between friend and foe through the perception of these signals is a major challenge. We report the synthesis of a range of COs and LCOs, including photoactivatable probes, to characterize a membrane protein from the legume Medicago truncatula. By coupling photoaffinity labeling experiments with proteomics and transcriptomics, we identified the likely LCO-binding protein as LYR3, a lysin motif receptor-like kinase (LysM-RLK). LYR3, expressed heterologously, exhibits high-affinity binding to LCOs but not COs. Homology modeling, based on the Arabidopsis CO-binding LysM-RLK AtCERK1, suggests that LYR3 could accommodate the LCO in a conserved binding site. The identification of LYR3 opens up ways for the molecular characterization of LCO/CO discrimination.
Methods: SDS-PAGE, radiolabeling, molecular modeling, photoaffinity labeling, autoradiography Biological activity: confirmed affinity to LYR3, LysM-RLK of M. truncatula Synthetic data: enzymatic in vivo Comments, role: Oligosaccharide is associated with the formation of the mycorrhiza 3D data: computer modelling
The structure was elucidated in this paper NCBI PubMed ID:23808871 Publication DOI:10.1021/cb400369u Journal NLM ID:101282906 Publisher: Washington, DC: American Chemical Society Correspondence: Jean-Jacques.Bonotoulouse.inra.fr Institutions: INRA, Laboratoire des Interactions Plantes-Microorganismes (LIPM), Castanet-Tolosan, France, CNRS, Laboratoire des Interactions Plantes-Microorganismes (LIPM), Castanet-Tolosan, France, Université Paris-Sud and CNRS, Laboratoire de Synthèse de Biomolécules, Institut de Chimie Moléculaire et des Matériaux d’Orsay, Orsay, France, Université de Toulouse, Laboratoire de Recherche en Sciences Végétales (LRSV), Castanet-Tolosan, France, CNRS, Castanet-Tolosan, France, Plateforme de Protéomique, Toulouse, France, Centre de Recherches sur les Macromolécules Végétales, Grenoble, France, Centre de Recherche de Gif, Institut de Chimie des Substances Naturelles du CNRS, Gif-sur-Yvette,France, School of Pharmaceutical Sciences, Geneva, Switzerland
While chitooligosaccharides (COs) derived from fungal chitin are potent elicitors of defense reactions, structurally related signals produced by certain bacteria and fungi, called lipo-chitooligosaccharides (LCOs), play important roles in the establishment of symbioses with plants. Understanding how plants distinguish between friend and foe through the perception of these signals is a major challenge. We report the synthesis of a range of COs and LCOs, including photoactivatable probes, to characterize a membrane protein from the legume Medicago truncatula. By coupling photoaffinity labeling experiments with proteomics and transcriptomics, we identified the likely LCO-binding protein as LYR3, a lysin motif receptor-like kinase (LysM-RLK). LYR3, expressed heterologously, exhibits high-affinity binding to LCOs but not COs. Homology modeling, based on the Arabidopsis CO-binding LysM-RLK AtCERK1, suggests that LYR3 could accommodate the LCO in a conserved binding site. The identification of LYR3 opens up ways for the molecular characterization of LCO/CO discrimination.
Methods: SDS-PAGE, radiolabeling, molecular modeling, photoaffinity labeling, autoradiography Biological activity: confirmed affinity to LYR3, LysM-RLK of M. truncatula Synthetic data: enzymatic in vivo Comments, role: Oligosaccharide is associated with the formation of the mycorrhiza 3D data: computer modelling
Ohana P, Delmer DP, Volman G, Benziman M Glycosylated triterpenoid saponin: a specific inhibitor of diguanylate cyclase from Acetobacter xylinum. Biological activity and distribution Plant and Cell Physiology39(2) (1998)
153-159
Taxonomic group: plant / Streptophyta (Phylum: Streptophyta) Organ / tissue:seed
Publication DOI:10.1093/oxfordjournals.pcp.a029352 Journal NLM ID:9430925 Publisher: Tokyo: Oxford University Press Institutions: Section of Plant Biology, University of California Davis, Davis, US, Department of Biological Chemistry, Institute of Life Sciences, The Hebrew University of Jerusalem, Israel
In a recent paper (Ohana et al. 1998), we described the purification and structural characterization of a novel glycosidic triterpenoid saponin (GTS), a specific inhibitor of diguanylate cyclase (dgc), the key regulatory enzyme of the cellulose synthesizing apparatus of the bacterium Acetobacter xylinum, This compound and an identical or very similar one were isolated from pea (Pisum sativum), and A. xylinum respectively, We now present the effects of GTS on the kinetic properties of dgc. The observed inhibition is non-competitive with respect to the substrate GTP, is decreased by 50% in the presence of 20 mu M c-di-GMP, and is not observed in the presence of various detergents. Photoaffinity labeling studies using [P-32]c-di-GMP and purified enzyme showed that the inhibitor affects binding of c-di-GMP to dgc, It was ascertained that GTS, or at least a very similar compound, is present in other plant systems, The antibiotic Papulacandin B also inhibits dgc, although less efficiently than GTS (Ki=70 mu M vs. 5 mu M). In in situ assays, highly purified GTS inhibits bacterial cellulose synthesis and dgc activity, Similary, digitonin permeabilized tobacco cell cultures display inhibition of glucan synthesis in the presence of GTS.
Methods: inhibition studies, biological assays, photoaffinity labeling Biological activity: inhibits diguanylate cyclase of Acetobacter xylinum; concentration of 5 μM is required for 50% inhibition of enzyme; in the presence of GTS cellulose synthesis in A. xylinum was inhibited on 70%
Found 
report error
toulouse.inra.fr