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Glycerol is an important osmotically compatible solute in  Dunaliella . Glycerol-3-phosphate dehydrogenase (G3PDH) is a key enzyme in the pathway of glycerol synthesis, which converts dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate. Generally, the glycerol-DHAP cycle pathway, which is driven by G3PDH, is considered as the rate-limiting enzyme to regulate the glycerol level under osmotic shocks. Considering the peculiarity in osmoregulation, the cDNA of a NAD + -dependent  G3PDH  was isolated from  D. salina  using RACE and RT-PCR approaches in this study. Results indicated that the length of the cDNA sequence of  G3PDH  was 2,100 bp encoding a 699 amino acid deduced polypeptide whose computational molecular weight was 76.6 kDa. Conserved domain analysis revealed that the G3PDH protein has two independent functional domains, SerB and G3PDH domains. It was predicted that the G3PDH was a nonsecretory protein and may be located in the chloroplast of  D. salina . Phylogenetic analysis demonstrated that the  D. salina  G3PDH had a closer relationship with the G3PDHs from the  Dunaliella  genus than with those from other species. In addition, the cDNA was subsequently subcloned in the pET-32a(+) vector and was transformed into  E. coli  strain BL21 (DE3), a expression protein with 100 kDa was identified, which was consistent with the theoretical value.

Molecular Clone and Expression of a NAD+-Dependent Glycerol-3-Phosphate Dehydrogenase Isozyme Gene from the Halotolerant alga Dunaliella salina