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Targeted Gene Disruption of OsCERK1 Reveals Its Indispensable Role in Chitin Perception and Involvement in the Peptidoglycan Response and Immunity in Rice

September 2014 , Volume 27 , Number  9
Pages  975 - 982

Yusuke Kouzai,1 Susumu Mochizuki,1 Keisuke Nakajima,1 Yoshitake Desaki,2 Masahiro Hayafune,2 Hideo Miyazaki,2 Naoki Yokotani,1 Kenjirou Ozawa,1 Eiichi Minami,1 Hanae Kaku,2 Naoto Shibuya,2 and Yoko Nishizawa1

1Genetically Modified Organism Research Center, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki, 305-8602 Japan; 2Department of Life Sciences, School of Agriculture, Meiji University, Tama-ku, Kawasaki, Kanagawa, 214-8571 Japan

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Accepted 26 May 2014.

OsCERK1 is a rice receptor-like kinase that mediates the signal of a fungal cell wall component, chitin, by coordinating with a lysin motif (LysM)-containing protein CEBiP. To further elucidate the function of OsCERK1 in the defense response, we disrupted OsCERK1 using an Agrobacterium-mediated gene targeting system based on homologous recombination. In OsCERK1-disrupted lines, the generation of hydrogen peroxide and the alteration of gene expression in response to a chitin oligomer were completely abolished. The OsCERK1-disrupted lines also showed lowered responsiveness to a bacterial cell wall component, peptidoglycan. Yeast two-hybrid analysis indicated that OsCERK1 interacts with the LysM-containing proteins LYP4 and LYP6, which are known to participate in the peptidoglycan response in rice. Observation of the infection behavior of rice blast fungus (Magnaporthe oryzae) revealed that disruption of OsCERK1 led to increased hyphal growth in leaf sheath cells. Green fluorescent protein-tagged OsCERK1 was localized around the primary infection hyphae. These results demonstrate that OsCERK1 is indispensable for chitin perception and participates in innate immunity in rice, and also mediates the peptidoglycan response. It is also suggested that OsCERK1 mediates the signaling pathways of both fungal and bacterial molecular patterns by interacting with different LysM-containing receptor-like proteins.

© 2014 The American Phytopathological Society