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Molecular characterization of the cDNA encoding an acidic isoform of PR-1 protein in rice.

Rice cDNA encoding an acidic type of pathogenesis-related protein-1 (PR-1a) was cloned and characterized. The deduced PR-1a protein consisted of 168 amino acid residues, including 24 hydrophobic signal sequences at the N-terminus. The predicted molecular mass of the PR-1a was 15,728 Da with a theoretical pI of 4.5, an indication of an acidic protein. The PR-la showed high homology to an acidic PR-1 of Zea mays (74%) and a previously identified basic type PR-1 of rice (64%). Both rice PR-1 and PR-1a genes were found to exist as small gene families through Southern blot hybridization analyses. The PR-1 mRNA was accumulated only in leaves, while the PR-1a transcript was accumulated throughout the plant at a low level. Expression of both PR-1 genes was induced by infections of the rice blast fungus, Magnaporthe grisea, or the bacterial leaf blight pathogen, Xanthomonas oryzae pv. oryzae, and the treatment of benzo (1, 2, 3) thiadiazole-7-carbothioic acid S-ethyl ester, H2O2, or CuSO4. The expression of both PR-1 genes was higher and more rapidly induced in an incompatible interaction than in a compatible interaction in the rice M. grisea interactions.