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LYR 3, a high‐affinity LCO ‐binding protein of Medicago truncatula , interacts with LYK 3, a key symbiotic receptor
Author(s) -
Fliegmann Judith,
Jauneau Alain,
Pichereaux Carole,
Rosenberg Charles,
Gasciolli Virginie,
Timmers Antonius C.J.,
BurletSchiltz Odile,
Cullimore Julie,
Bono JeanJacques
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12191
Subject(s) - medicago truncatula , förster resonance energy transfer , receptor , bimolecular fluorescence complementation , microbiology and biotechnology , kinase , biology , chemistry , biochemistry , biophysics , fluorescence , gene , bacteria , symbiosis , genetics , physics , quantum mechanics
LYR3, LYK 3, and NFP are lysin motif‐containing receptor‐like kinases (LysM‐ RLK s) from Medicago truncatula, involved in perception of symbiotic lipo‐chitooligosaccharide ( LCO ) signals. Here, we show that LYR 3, a high‐affinity LCO ‐binding protein, physically interacts with LYK 3, a key player regulating symbiotic interactions. In vitro , LYR 3 is phosphorylated by the active kinase domain of LYK 3. Fluorescence lifetime imaging/Förster resonance energy transfer ( FLIM / FRET ) experiments in tobacco protoplasts show that the interaction between LYR 3 and LYK 3 at the plasma membrane is disrupted or inhibited by addition of LCO s. Moreover, LYR 3 attenuates the cell death response, provoked by coexpression of NFP and LYK 3 in tobacco leaves.