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Requirement for phospholipids of the translocation of the trimethylamine N ‐oxide reductase through the Tat pathway in Escherichia coli
Author(s) -
Mikhaleva Nathalia I.,
Santini Claire-Lise,
Giordano Gérard,
Nesmeyanova Marina A.,
Wu Long-Fei
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01661-0
Subject(s) - escherichia coli , biochemistry , twin arginine translocation pathway , chromosomal translocation , phosphatidylethanolamine , mutant , chemistry , phospholipid , trimethylamine , trimethylamine n oxide , reductase , enzyme , phosphatidylcholine , membrane transport protein , membrane protein , membrane , gene
Trimethylamine N ‐oxide reductase (TorA) is an anaerobically synthesized molybdoenzyme. It is translocated across the cytoplasmic membrane in a folded conformation via the Tat pathway of Escherichia coli . The requirement for phospholipids for the export of this enzyme was analyzed in the pgsA and pss mutants lacking anionic phospholipids and phosphatidylethanolamine, respectively. Anaerobic growth did not influence phospholipid composition of the pgsA and pss mutants. Interestingly, both pgsA and pss mutations severely retarded the translocation of TorA into the periplasm. Therefore, translocation of proteins through the Tat pathway is dependent on the anionic phospholipids and on lipid polymorphism.