Abstract
O. brevis bxa1 gene encoding a CPx-ATPase has been characterized in our group. To clarify the gene function for Cd stress in more detail, experiments were performed using the constructed yeast transformants.
The bxa1 transformant was more sensitive to Cd than a control carrying a vector. Expression of the bxa1 also resulted in morphological changes. Moreover, Bxa1::GFP fusion protein was localized mainly in endoplasmic reticulum (ER). Localization of Bxa1 in ER may decline the function of ER and cause the differences in Cd sensitivity and the morphological changes. To investigate the role of N-terminal domain in Bxa1, yeast transformants carrying the two deletion plasmids (Δ10 or Δ35AA Bxa1) were characterized. Deletion of the N-terminal domain in Bxa1 led to a change of the Cd sensitivity and yeast growth. These results suggest that the domain may be involved in the regulation of Cd transport.
