Molecular characterization of a catalase gene in the freshwater green alga Closterium ehrenbergii and its putative function against abiotic stresses

Abstract

Catalases (CATs) are ubiquitous antioxidant enzymes that prevent cellular oxidative damage through the decomposition of H2O2. However, there is relatively little information on CAT in the worldwide-distributed freshwater green alga Closterium ehrenbergii. Here, we cloned the full-length catalase cDNA from C. ehrenbergii (CeCAT) and characterized its structural features and expressional responses against aquatic contaminants. The open reading frame of CeCAT was determined to be 1476 bp, encoding 491 amino acids with a theoretical molecular mass of 56.1 kDa. The CeCAT protein belongs to the NADPH-binding CAT family and might be located in the cytosol. BLAST and phylogenetic results showed that CeCAT had a high identity with CAT proteins from other microalgae and the water lily Nymphaea colorata (Streptophyta). The transcriptional levels of CeCAT were significantly upregulated by the metal copper and herbicide atrazine, but little affected by other tested metals (Ni and Cr) and endocrine-disrupting chemicals (polychlorinated biphenyl, PCB). The maximum expression was registered under 0.1 mg/L CuCl2 and 0.2 mg/L CuSO4 exposures. In addition, excess copper considerably increased production of reactive oxygen species in the cells. These results suggest that CeCAT may function to defend against oxidative stress in green algae and can respond specifically to different kinds of metals and herbicides.