The recombinant E. coli O6:H1 aqpZ protein is produced using a cell-free in vitro expression system. This system utilizes E. coli extracts containing the necessary components for protein synthesis, including transcription, translation, and post-translational modifications. The aqpZ protein is synthesized in vitro within hours by supplementing the cell extracts with cofactors. While this method offers advantages like rapid synthesis and simultaneous expression of multiple proteins, it may not be suitable for large-scale production.
aqpZ, a member of the aquaporin family, is renowned for its small size, simple structure, and robust function. It exhibits high selectivity for water transport, ensuring efficient water movement across cell membranes. Following reconstitution into polymeric bilayer membrane vesicles, aqpZ retains its characteristic water permeability. This protein plays a crucial role in both short-term and long-term osmoregulation, particularly essential for rapidly growing cells. The unique hourglass configuration of aqpZ, featuring the NPA motif, contributes to its exceptional water selectivity and near-complete salt rejection.