Activation of members of a MAPK module in β-glucan elicitor-mediated non-host resistance of soybean

被引:25
作者
Daxberger, Andrea
Nemak, Andrea
Mithoefer, Axel
Fliegmann, Judith
Ligterink, Wilco
Hirt, Heribert
Ebel, Juergen
机构
[1] Univ Munich, Dept Biol Bot 1, D-80638 Munich, Germany
[2] Max Planck Inst Chem Okol, D-07745 Jena, Germany
[3] Univ Vienna, Max F Perutz Labs, Dept Pflanzenmol Biol, A-1030 Vienna, Austria
关键词
beta-Glucan elicitors; glycine; mitogen-activated protein kinase (MAPK) signaling; phytophthora; protein interaction;
D O I
10.1007/s00425-006-0442-6
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Plants recognize microbial pathogens by discriminating pathogen-associated molecular patterns from self-structures. We study the non-host disease resistance of soybean (Glycine max L.) to the oomycete, Phytophthora sojae. Soybean senses a specific molecular pattern consisting of a branched heptaglucoside that is present in the oomycetal cell walls. Recognition of this elicitor may be achieved through a beta-glucan-binding protein, which forms part of a proposed receptor complex. Subsequently, soybean mounts a complex defense response, which includes the increase of the cytosolic calcium concentration, the production of reactive oxygen species, and the activation of genes responsible for the synthesis of phytoalexins. We now report the identification of two mitogen-activated protein kinases (MAPKs) and one MAPK kinase (MAPKK) that may function as signaling elements in triggering the resistance response. The use of specific antisera enabled the identification of GmMPKs 3 and 6 whose activity is enhanced within the signaling pathway leading to defense reactions. Elicitor specificity of MAPK activation as well as the sensitivity against inhibitors suggested these kinases as part of the beta-glucan signal transduction pathway. An upstream GmMKK1 was identified based on sequence similarity to other plant MAPKKs and its interaction with the MAPKs was analyzed. Recombinant GmMKK1 interacted predominantly with GmMPK6, with concomitant phosphorylation of the MAPK protein. Moreover, a preferential physical interaction between GmMKK1 and GmMPK6 was demonstrated in yeast. These results suggest a role of a MAPK cascade in mediating beta-glucan signal transduction in soybean, similar to other triggers that activate MAPKs during innate immune responses in plants.
引用
收藏
页码:1559 / 1571
页数:13
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