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Proteomic analysis of differentially expressed proteins induced by rice blast fungus and elicitor in suspension‐cultured rice cells
Author(s) -
Kim Sun Tae,
Cho Kyu Seong,
Yu Seok,
Kim Sang Gon,
Hong Jong Chan,
Han Changdeok,
Bae Dong Won,
Nam Myung Hee,
Kang Kyu Young
Publication year - 2003
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200300577
Subject(s) - elicitor , proteome , biology , magnaporthe grisea , jasmonic acid , biochemistry , proteomics , western blot , fungus , microbiology and biotechnology , salicylic acid , gene , oryza sativa , botany
We used two‐dimensional electrophoresis (2‐DE) and other proteomic approaches to identify proteins expressed in suspension‐cultured rice cells in response to the rice blast fungus, Magnaporthe grisea . Proteins were extracted from suspension‐cultured cells at 24 and 48 h after rice blast fungus inoculation or treatment with elicitor or other signal molecules such as jasmonic acid (JA), salicylic acid, and H 2 O 2 . The proteins were then polyethylene glycol fractionated before separation by 2‐DE. Fourteen protein spots were induced or increased by the treatments, which we analyzed by N ‐terminal or internal amino acid sequencing. Twelve proteins from six different genes were identified. Rice pathogen‐related protein class 10 (OsPR‐10), isoflavone reductase like protein, β‐glucosidase, and putative receptor‐like protein kinase were among those induced by rice blast fungus; these have not previously been reported in suspension‐cultured rice cells. Six isoforms of probenazole‐inducible protein (PBZ1) and two isoforms of salt‐induced protein (SalT) that responded to blast fungus, elicitor, and JA were also resolved on a 2‐DE gel and identified by proteome analysis. The expression level of these induced proteins both in suspension‐cultured cells and in leaves of whole plants was analyzed by Western blot. PBZ1, OsPR‐10, and SalT proteins from incompatible reactions were induced earlier and to a greater extent than those in compatible reactions. Proteome analysis can thus distinguish differences in the timing and amount of protein expression induced by pathogens and other signal molecules in incompatible and compatible interactions.