A remorin protein interacts with symbiotic receptors and regulates bacterial infection
Author(s) -
Benoît Lefebvre,
Ton Timmers,
Malick Mbengué,
Sandra Moreau,
Christine Hervé,
Katalin Tóth,
Joana BittencourtSilvestre,
D. Klaus,
Laurent Deslandes,
Laurence Godiard,
Jeremy D. Murray,
Michael K. Udvardi,
Sylvain Raffaele,
Sébastien Mongrand,
Julie V. Cullimore,
Pascal Gamas,
Andréas Niebel,
Thomas Ott
Publication year - 2010
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0913320107
Subject(s) - medicago truncatula , rhizobia , biology , microbiology and biotechnology , symbiosis , signal transduction , cytoplasm , sinorhizobium meliloti , bacteria , receptor , host (biology) , genetics
Remorin proteins have been hypothesized to play important roles during cellular signal transduction processes. Induction of some members of this multigene family has been reported during biotic interactions. However, no roles during host-bacteria interactions have been assigned to remorin proteins until now. We used root nodule symbiosis between Medicago truncatula and Sinorhizobium meliloti to study the roles of a remorin that is specifically induced during nodulation. Here we show that this oligomeric remorin protein attaches to the host plasma membrane surrounding the bacteria and controls infection and release of rhizobia into the host cytoplasm. It interacts with the core set of symbiotic receptors that are essential for perception of bacterial signaling molecules, and thus might represent a plant-specific scaffolding protein.
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