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Taxonomic group: fungi / Mucoromycota (Phylum: Mucoromycota)

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.Bono

toulouse.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.

LOS, bacteria, legume, fungi, Nod-factors, mycorrhizae

Structure type: oligomer
Location inside paper: Fig. 1 (3), Myc LCO-IV(C16:0), Myc LCO-IV(S,C16:0), Myc LCO-IV(C18:1Δ9), Myc LCO-IV(S,C18:1Δ9)
Compound class: LOS
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141181,IEDB_141807,IEDB_142354,IEDB_151531,IEDB_153212,IEDB_1635956,IEDB_241099,IEDB_241119,IEDB_241120,SB_74,SB_85

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

Related record ID(s): 48518
NCBI Taxonomy refs (TaxIDs): 588596
Show glycosyltransferases

There is only one chemically distinct structure:

CCCCCCCC/C=C/CCCCCCCC(=O)N[C@H]1[C@H](O[C@@H]2[C@@H](CO)O[C@@H](O[C@@H]3[C@@H](CO)O[C@@H](O[C@@H]4[C@@H](COS(=O)(=O)O)O[C@@H](O)[C@H](NC(C)=O)[C@H]4O)[C@H](NC(C)=O)[C@H]3O)[C@H](NC(C)=O)[C@H]2O)O[C@H](CO)[C@@H](O)[C@@H]1O

SVG MW SMILES 3D mol Ionize

Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)

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.Bono

LOS, bacteria, legume, fungi, Nod-factors, mycorrhizae

Structure type: oligomer
Location inside paper: Fig. 1 (1, 2) NodSm-IV(S), NodSm-IV(Ac, S)
Compound class: LOS
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_142354,IEDB_151531,IEDB_153212,IEDB_1635956,IEDB_241099,IEDB_241119,IEDB_241120,SB_74,SB_85

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

Related record ID(s): 44848
NCBI Taxonomy refs (TaxIDs): 382
Show glycosyltransferases

There is only one chemically distinct structure:

$CCCCCC/C=C\CCCCC/C=C/C(=O)N[C@H]1[C@H](O[C@@H]2[C@@H](CO)O[C@@H](O[C@@H]3[C@@H](CO)O[C@@H](O[C@@H]4[C@@H](COS(=O)(=O)O)O[C@@H](O)[C@H](NC(C)=O)[C@H]4O)[C@H](NC(C)=O)[C@H]3O)[C@H](NC(C)=O)[C@H]2O)O[C@H](CO)[C@@H](O)[C@@H]1O$

SVG MW SMILES 3D mol Ionize

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.

Acetobacter xylinum, Pisum sativum, c-di-GMP, dgc, GTS

Structure type: oligomer
Location inside paper: GTS, ref.[Ohana et al. 1998]
Compound class: triterpenoid glycoside
Contained glycoepitopes: IEDB_115136,IEDB_136044,IEDB_136105,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_142488,IEDB_146664,IEDB_190606,IEDB_225177,IEDB_423153,IEDB_885823,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88

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%

Related record ID(s): 61486
NCBI Taxonomy refs (TaxIDs): 3888
Show glycosyltransferases

There is only one chemically distinct structure:

C[C@@H]1O[C@@H](O[C@H]2[C@H](O[C@@H]3[C@@H](O)[C@H](O)[C@@H](C(=O)O)O[C@H]3O[C@H]3CC[C@@]4(C)[C@@H](CC[C@]5(C)[C@@H]4CC=C4[C@@H]6CC(C)(C)C[C@@H](O[C@@H]7O[C@H](CO)[C@@H](O)[C@H](O)[C@H]7O)[C@]6(C)CC[C@]45C)[C@@]3(C)CO)O[C@H](CO)[C@H](O)[C@@H]2O)[C@H](O)[C@H](O)[C@H]1O

SVG MW SMILES 3D mol Ionize