Molecular cloning and oxidative-stress responses of a novel Phi class glutathione S-transferase (GSTF) gene in the freshwater algae Closterium ehrenbergii.

Glutathione S-transferases (GSTs) belong to a family of enzymes involved in diverse biological processes, including detoxification and protection against oxidative damage. Here, we determined the full-length sequence (915 bp) of a novel Phi class cytosolic glutathione S-transferase (GSTF) gene from the green algae Closterium ehrenbergii. We examined the gene structure and expression patterns in response to metals and endocrine disrupting chemicals (EDCs). It was significantly upregulated by metals, but responded differently to EDCs. The highest up-regulation of CeGSTF was registered under 0.1 mg/L CuCl 2 and 0.01 mg/L CuSO 4 treatments. In a 72-h course experiment with treatment of 0.1 mg/L CuCl 2 , CeGSTF was dramatically induced at 6 h, and then gradually decreased with increasing exposure time. This was consistent with the increase in both GST activity and ROS production in copper-treated cells. These results suggest that CeGSTF may be involved in detoxification mechanisms associated with oxidative stress in green algae.