Our aim was to transport Vitamin B12, a substance which has no known cellular exporter in nature, through the inner membrane out of the cytoplasm.
Our different B12 Synporter proteins consist of TorA signal peptide for a Twin Arginine Transporter (Tat) mediated export that is linked to a B12-binding domain. This construct was produced, together with B12, by the B12 autotrophic R. planticola and S. blattae. First, we could show that the Synporter proteins were translocated into the periplasm. Moreover, most important, we could also prove the enrichment of B12 in the periplasm, which proofs that our Synporter is functional.
Thereby, Vitamin B12 can also be regarded as a prime example we wanted to state with our work. In principle, a Synporter should work with basically any chemical (that can form a non-covalent bond to a protein), which is desired to be exported out of a cell. This is the first time reported that a high-molecular compound as B12 was translocated through a cellular membrane, which makes our Synporter so innovative.
This concept can be applied for the production of all natural chemicals which are synthesized, but not exported due to the lack of a cellular exporter. Furthermore, it can also be applied for the production of artificial molecules which can be produced by synthetic metabolic engineering in a cell. Using our Synporter approach, no cell lysis is required any more for the industrial production, which makes the production process significantly easier and cheaper.
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