| Autor: |
Fliegmann J; INRA , Laboratoire des Interactions Plantes-Microorganismes (LIPM), UMR441, 31326 Castanet-Tolosan, France., Canova S, Lachaud C, Uhlenbroich S, Gasciolli V, Pichereaux C, Rossignol M, Rosenberg C, Cumener M, Pitorre D, Lefebvre B, Gough C, Samain E, Fort S, Driguez H, Vauzeilles B, Beau JM, Nurisso A, Imberty A, Cullimore J, Bono JJ |
| Jazyk: |
angličtina |
| Zdroj: |
ACS chemical biology [ACS Chem Biol] 2013 Sep 20; Vol. 8 (9), pp. 1900-6. Date of Electronic Publication: 2013 Jul 05. |
| DOI: |
10.1021/cb400369u |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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