A receptor kinase gene of the LysM type is involved in legumeperception of rhizobial signals

Esben Bjørn Madsen, Lene Heegaard Madsen, Simona Radutoiu, Magdalena Olbryt, Magdalena Rakwalska, Krzysztof Szczyglowski, Shusei Sato, Takakazu Kaneko, Satoshi Tabata, Niels Sandal and Jens Stougaard ()
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Esben Bjørn Madsen: University of Aarhus
Lene Heegaard Madsen: University of Aarhus
Simona Radutoiu: University of Aarhus
Magdalena Olbryt: University of Aarhus
Magdalena Rakwalska: University of Aarhus
Krzysztof Szczyglowski: Agriculture and Agri-Food Canada, SCPFRC
Shusei Sato: Kazusa DNA Research Institute
Takakazu Kaneko: Kazusa DNA Research Institute
Satoshi Tabata: Kazusa DNA Research Institute
Niels Sandal: University of Aarhus
Jens Stougaard: University of Aarhus

Nature, 2003, vol. 425, issue 6958, 637-640

Abstract: Abstract Plants belonging to the legume family develop nitrogen-fixing root nodules in symbiosis with bacteria commonly known as rhizobia. The legume host encodes all of the functions necessary to build the specialized symbiotic organ, the nodule, but the process is elicited by the bacteria1,2,3. Molecular communication initiates the interaction, and signals, usually flavones, secreted by the legume root induce the bacteria to produce a lipochitin-oligosaccharide signal molecule (Nod-factor), which in turn triggers the plant organogenic process4,5,6,7. An important determinant of bacterial host specificity is the structure of the Nod-factor, suggesting that a plant receptor is involved in signal perception and signal transduction initiating the plant developmental response8,9. Here we describe the cloning of a putative Nod-factor receptor kinase gene (NFR5) from Lotus japonicus. NFR5 is essential for Nod-factor perception and encodes an unusual transmembrane serine/threonine receptor-like kinase required for the earliest detectable plant responses to bacteria and Nod-factor. The extracellular domain of the putative receptor has three modules with similarity to LysM domains known from peptidoglycan-binding proteins and chitinases. Together with an atypical kinase domain structure this characterizes an unusual receptor-like kinase.

Date: 2003
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DOI: 10.1038/nature02045

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