Requirement for phospholipids of the translocation of the trimethylamine N-oxide reductase through the Tat pathway in Escherichia coli

Trimethylamine N-oxide reductase (TorA) is an anaerobically synthesized mol ybdoenzyme. It is translocated across the cytoplasmic membrane in a folded conformation via the Tat pathway of Escherichia coli, The requirement for p hospholipids for the export of this enzyme was analyzed in the pgsA and pss mutants lacking anionic phospholipids and phosphatidylethanolamine, respec tively. Anaerobic growth did not influence phospholipid composition of the pgsA and pss mutants, Interestingly, both pgsA and pss mutations severely r etarded the translocation of TorA into the periplasm, Therefore, translocat ion of proteins through the Tat pathway is dependent on the anionic phospho lipids and on lipid polymorphism. (C) 1999 Federation of European Biochemic al Societies.