Contribution to a Sustainable Society: Biosorption of Precious Metals Using the Microalga Galdieria.

The red microalga Galdieria sp. is an extremophile that inhabits acidic hot sulphur springs and grows heterotrophically to a high cell density. These characteristics make Galdieria suitable for commercial applications as stable mass production is the key to success in the algae business. Galdieria has great potential as a precious metal adsorbent to provide a sustainable, efficient and environmentally benign method for urban mining and artisanal small-scale gold mining. The efficiency and selectivity in capturing precious metals, gold and palladium from metal solutions by a Galdieria-derived adsorbent was assessed relative to commercially used adsorbents, ion exchange resin and activated charcoal. As it is only the surface of Galdieria cells that affect metal adsorption, the cell content was analysed to determine the manner of utilisation of those metabolites. Galdieria was shown to be protein-rich and contain beneficial metabolites, the levels of which could shift depending on the growth conditions. Separating the cell content from the adsorbent could improve the adsorption efficiency and reduce CO2 emissions during the metal collection process. The commercial applications of Galdieria appear promising: growth is quick and dense; the precious metal adsorption capacity is highly efficient and selective in acidic conditions, especially at low metal concentrations; and the cell content is nutrient-rich.

Coordinated upregulation of two CDP-diacylglycerol synthases, YnbB and CdsA, is essential for cell growth and membrane protein export in the cold.

YnbB is a paralogue of CdsA, a CDP-diacylglycerol synthase. While the cdsA gene is essential, the ynbB gene is dispensable. So far, no phenotype of ynbB knockout has been observed. We found that a ynbB knockout strain acquired cold-sensitivity on growth under CdsA-limited conditions. We found that MPIase, a glycolipid involved in protein export, is cold-upregulated to facilitate protein export in the cold, by increasing the mRNA levels of not only CdsA but also that of YnbB. Under non-permissive conditions, phospholipid biosynthesis proceeded normally, however, MPIase upregulation was inhibited with accumulation of precursors of membrane and secretory proteins such as M13 procoat and proOmpA, indicating that YnbB is dedicated to MPIase biosynthesis, complementing the CdsA function.

Biosynthesis of glycolipid MPIase (membrane protein integrase) is independent of the genes for ECA (enterobacterial common antigen).

MPIase (membrane protein integrase) is an essential glycolipid that drives protein integration into the inner membrane of E. coli, while glycolipid ECA (enterobacterial common antigen) is a major component at the surface of the outer membrane. Irrespective of the differences in molecular weight, subcellular localization and function in cells, the glycan chains of the two glycolipids are similar, since the repeating unit comprising the glycan chains is the same. A series of biosynthetic genes for ECA, including ones for the corresponding nucleotide sugars, have been identified and extensively characterized. In this study, we found that knockouts as to the respective genes for ECA biosynthesis can grow in the minimum medium with the normal expression level of MPIase, indicating that MPIase can be biosynthesized de novo without the utilization of any compounds generated through ECA biosynthesis. Conversely, ECA was expressed normally upon MPIase depletion. From these results, we conclude that the biosynthetic genes for MPIase and ECA are independent.

CdsA is involved in biosynthesis of glycolipid MPIase essential for membrane protein integration in vivo.

MPIase is a glycolipid that is involved in membrane protein integration. Despite evaluation of its functions in vitro, the lack of information on MPIase biosynthesis hampered verification of its involvement in vivo. In this study, we found that depletion of CdsA, a CDP-diacylglycerol synthase, caused not only a defect in phospholipid biosynthesis but also MPIase depletion with accumulation of the precursors of both membrane protein M13 coat protein and secretory protein OmpA. Yeast Tam41p, a mitochondrial CDP-diacylglycerol synthase, suppressed the defect in phospholipid biosynthesis, but restored neither MPIase biosynthesis, precursor processing, nor cell growth, indicating that MPIase is essential for membrane protein integration and therefore for cell growth. Consistently, we observed a severe defect in protein integration into MPIase-depleted membrane vesicles in vitro. Thus, the function of MPIase as a factor involved in protein integration was proven in vivo as well as in vitro. Moreover, Cds1p, a eukaryotic CdsA homologue, showed a potential for MPIase biosynthesis. From these results, we speculate the presence of a eukaryotic MPIase homologue.