Al SerB domains [20,26]. It has been reported that such bi-domain G

Al SerB domains [20,26]. It has been reported that such bi-domain G3PDHs only exist in green alga, but not in larger plants or other species, which include yeasts and animals [26]. One example is, only one catalytic domain has been discovered exist in polypeptide chain of G3PDHs in yeasts Debaryomyces hansenii, Candida glycerinogenes and Candidamagnoliae [335]. The existence of distinctive bi-domain G3PDHs in these green algae might be the evolutionary consequence, which maintained a exceptional osmoregulation mechanism in green algae for survival in extreme environments [26]. Some essential enzyme genes associated to glycerol metabolism, such as the cDNA of fructose-1, 6-diphosphate aldolase (DsALDP) and NAD+-G3PDH are cloned from D. salina. These genes have been transferred into bacteria or plants to improve the salt-tolerance of these species. Zhang et al transferred the DsALDP gene into E.6α-Methylprednisolone 21-hemisuccinate sodium salt coli cultured in media with various NaCl concentration to analyze its expression [36]. As a result, the bacteria expressing DsALDP exhibited a greater salt tolerance with increasing NaCl concentration than bacteria with no DsALDP expression.Phenanthriplatin In addition, Zhang et al transferred the DsALDP gene into tobacco by Agrobacterium tumefaciens, and DsALDP gene was expressed effectively in transgenic tobacco, which exhibited a higher salt tolerance [37]. In yet another report, a G3PDH gene from D. salina has been transferred into led discs cells of tobacco. RT-PCR analysisCharacterization of GPHD Gene from D. salinashowed that G3PDH gene integrated into tobacco genome has made mRNA [38]. In the present study, the prokaryotic expression vector pET-32a-G3pdh was constructed and transferred into E. coli strain BL21 (DE3). The evaluation by SDS-PAGE showed that the G3PDH protein was expressed effectively in transgenic strains, plus the further work would emphasize on transforming this G3PDH gene into other greater plants to enhance their salt tolerance. In conclusion, in the present study the cDNA of a NAD+G3PDH was effectively isolated from D. salina. The cDNA was 2100 bp long, which encoded a deduced protein sequence of 699 amino acids with an estimated molecular weight of 76.6 kDa. Protein domain evaluation revealed that G3PDH protein has two independent functional domains, SerB and G3PDH domains.PMID:28038441 The D. salina G3PDH was a nonsecretory protein that may very well be located in the chloroplast. The D. salina G3PDH had a closer connection with Dunaliella G3PDHs than with these of other species in thephylogenetic analysis. The secondary and three-dimensional structure in the D. salina G3PDH is predicted. Moreover, the prokaryotic expression vector pET-32a-G3pdh was constructed and transferred into E. coli, in which G3PDH protein was expressed successfully. To totally fully grasp glycerol metabolism and osmotic adjustment determined by glycerol in Dunaliella, future investigation really should focus on the gene clone of some enzymes related to glycerol metabolism plus the application of transgenic technologies to increase salt-tolerance of other plants by transferring these cloned genes.Author ContributionsConceived and designed the experiments: MC. Performed the experiments: MC L-HH. Analyzed the information: MC. Contributed reagents/ materials/analysis tools: T-YY. Wrote the paper: MC T-YY.
Brief CommuniCationShort CommuniCationPlant Signaling Behavior eight, e27141; november; 2013 Landes BioscienceLipid droplet-associated proteins (LDAPs) are involved in the compartmentalization of lipophilic compounds in plant cellsSatinder K.