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- Title
Characterization of the wound-inducible protein ipomoelin from sweet potato.
- Authors
Chen, Y.-C.; Chang, H.-S.; Lai, H.-M.; Jeng, S.-T.
- Abstract
The ipomoelin (IPO) gene, a wound- and methyl jasmonate-inducible gene, was isolated from sweet potato (Ipomoea batatascv.Tainung57), and previously demonstrated to be regulated by dephosphorylated proteins and calcium ion (Chen Y.-C.et al.Plant Cell and Environment26, 1373–1383, 2003). In this report, the function of the IPO protein was further studied. The IPO gene was characterized as having one intron and presenting two copies within the genome of sweet potato. The IPO protein appeared 1 d after the leaves of sweet potato were wounded. Surprisingly, the accumulation of the IPO protein remained for 7 d after wounding. Additionally, after the IPO protein was fused to ahistidine tag, the His-IPO fusion protein produced fromEscherichia coliBL21DE3 was then used to perform the haemagglutination test, which demonstrated that His-IPO fusion protein agglutinated human blood cells. Furthermore, several carbohydrates, including methylα-d-glucopyranoside, methylα-d-mannopyranoside, maltose, mannose, glucose, galactose, and lactose, reduced the efficiency of the His-IPO fusion protein in agglutinating human blood cells. These experimental results may indicate that the IPO protein is alectin, a carbohydrate-binding protein. Notably, the IPO protein retarded the growth and development of silkworm, and thus reduced silkworm survival rates. Therefore, these findings indicate that the function of the IPO protein is to protect plants from insect attack.
- Subjects
PHYSICAL &; theoretical chemistry; BLOOD cells; ANTIGEN-antibody reactions; AGGLUTINATION tests; CARRIER proteins; BIOMOLECULES
- Publication
Plant, Cell & Environment, 2005, Vol 28, Issue 2, p251
- ISSN
0140-7791
- Publication type
Article
- DOI
10.1111/j.1365-3040.2005.01271.x