Plant Biotechnology Reports

The Korean Society of Plant Biotechnology (한국식물생명공학회)
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Proteomic analysis of rice mutants susceptible to Magnaporthe oryzae

  • Ryu, Hak-Seung (Graduate School of Biotechnology and Plant Metabolism Research Center, Kyung Hee University) ;
  • Song, Min-Young (Graduate School of Biotechnology and Plant Metabolism Research Center, Kyung Hee University) ;
  • Kim, Chi-Yeol (Graduate School of Biotechnology and Plant Metabolism Research Center, Kyung Hee University) ;
  • Han, Muho (Graduate School of Biotechnology and Plant Metabolism Research Center, Kyung Hee University) ;
  • Lee, Sang-Kyu (Graduate School of Biotechnology and Plant Metabolism Research Center, Kyung Hee University) ;
  • Ryoo, Nayeon (Graduate School of Biotechnology and Plant Metabolism Research Center, Kyung Hee University) ;
  • Cho, Jung-Il (Graduate School of Biotechnology and Plant Metabolism Research Center, Kyung Hee University) ;
  • Hahn, Tae-Ryong (Graduate School of Biotechnology and Plant Metabolism Research Center, Kyung Hee University) ;
  • Jeon, Jong-Seong (Graduate School of Biotechnology and Plant Metabolism Research Center, Kyung Hee University)
  • Received : 2009.03.02
  • Accepted : 2009.03.09
  • Published : 2009.04.30
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Abstract

To identify genes involved in rice Pi5-mediated disease resistance to Magnaporthe oryzae, we compared the proteomes of the RIL260 rice strain carrying the Pi5 resistance gene with its susceptible mutants M5465 and M7023. Proteins were extracted from the leaf tissues of both RIL260 and the mutant lines at 0, 24, and 48 h after M. oryzae inoculation and separated by two-dimensional polyacrylamide gel electrophoresis (2-DE). Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) analysis identified eight proteins that were differently expressed between the resistant and susceptible plants (three down- and five up-regulated proteins in the mutants). The down-regulated proteins included a triosephosphate isomerase (spot no. 2210), a 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (no. 3611), and an unknown protein (no. 4505). In addition, the five up-regulated proteins in the mutants were predicted to be a fructokinase I (no. 313), a glutathione S-transferase (no. 2310), an atpB of chloroplast ATP synthase (no. 3616), an aminopeptidase N (no. 3724), and an unknown protein (no. 308). These results suggest that proteomic analysis of rice susceptible mutants is a useful method for identifying novel proteins involved in resistance to the M. oryzae pathogen.

Keywords

Acknowledgement

Supported by : Ministry of Education, Science and Technology

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