Treatment of sweet potato plants cultured in vitro with a vapor of methyl jasmonate (MeJA) induced an accumulation in leaves of a large amount of protein with an apparent molecular mass of 18 kDa. This protein, designated ipomoelin, was purified, and the amino acid sequences of proteolytic fragments were determined. Screening a cDNA library of MeJA-treated leaves by oligonucleotide probes designed from the peptide sequences identified a clone that could code for a polypeptide with 154 amino acids. The deduced amino acid sequence of ipomoelin showed an overall amino acid identity of 25% with the salt-inducible SalT protein of rice. In addition, the C-terminal 70 amino acid sequence of ipomoelin showed about 50% identity with the C-terminal amino acid sequences of seed lectins from Moraceae. The gene for ipomoelin was present in a few copies in the genome of sweet potato. The mRNA for ipomoelin was detected in leaves and petioles, but not in stems and tuberous roots, of sweet potato plants grown in the field. Mechanical wounding of leaves induced ipomoelin mRNA both locally and systemically, while treatment of leaves with ABA, salt, or a high level of sucrose did not induce ipomoelin mRNA. By contrast, ABA-inducible mRNA for sporamin was not induced by MeJA. These results suggest that ipomoelin is involved in defensive reactions of leaves in response to wounding and that JA-mediated wound-induction of ipomoelin occurs independently of ABA.
|Number of pages||10|
|Journal||Plant and Cell Physiology|
|Publication status||Published - Jun 1997|
All Science Journal Classification (ASJC) codes
- Plant Science
- Cell Biology