z-logo
Premium
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 , microbiology and biotechnology , bimolecular fluorescence complementation , chemistry , receptor , kinase , biophysics , biology , biochemistry , 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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom