Plant and Cell Physiology Supplement
Abstract of the Annual Meeting of JSPP 2009
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Characterization of CEBiP2 possessed a structure similarity with chitin elicitor receptor in rice cells.
*Hideo MiyazakiMasanori HigashikawaAyako KatoYoko NishizawaNaoko Minami-IshiiEiichi MinamiHanae KakuNaoto Shibuya
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Pages 0979

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Abstract
CEBiP as a receptor plays an important role for chitin specific elicitor signaling in rice cells. However, the result from microarray analysis of CEBiP-RNAi suggests that the possibility of other molecule also assist the same function as like CEBiP. Meanwhile, we found a minor protein, named CEBiP2, was co-purified with CEBiP by (GlcNAc)8-Sepharose. CEBiP2 is a membrane glycoprotein consisted with two LysM motif in extracellular and three amino residues in intercellular domain, which showed the high structure similarity with CEBiP. To survey the function of CEBiP2, we prepared the CEBiP2 specific over-expression and knock down transformated rice cell. The result shows that CEBiP2 possesses the chitin elicitor binding activity. Moreover, the CEBiP2 specific knock-down cell lines were reduced the generation of chitin elicitor specific induced ROS. These results indicate that CEBiP2 may also play a same function as same as CEBiP.
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© 2009 by The Japanese Society of Plant Physiologists
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