Abstract
Ferritin is a multimeric iron storage protein. We presented that ferritin in the soybean seed contained two types of subunits, H-1 and H-2. The C-terminal domain of H-1 was cleaved and degraded completely, whereas the H-2, which we newly identified, was not subject to such cleavage in vitro. To examine the stability and capacity in iron storage of them, we use two types of transgenic tobacco, which express the H-1 and H-2 ferritin, respectively.
The iron content of the H-1 transgenic tobacco is higher than that of the H-1 when they grow in iron rich conditions. The stability assay is performed by the western blot using the antibody which recognize both H-1 and H-2 subunit. As the result, H-2 subunit was stable than the case of H-1 subunit. These results suggest that the H-2 subunit can be retained more stably and store iron efficienctly in the transgenic tobacco.
