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

FEBS Letters

Giordano, Gérard¹  Mikhaleva, Nathalia I.¹  Santini, Claire-Lise¹  Wu, Long-Fei¹  Nesmeyanova, Marina A.² 

[1] Laboratoire de Chimie Bactérienne, UPR9043 CNRS, Institut de Biologie Structurale et Microbiologie, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France;Laboratory of Protein Secretion in Bacteria, Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region 142292, Russia

关键词: Trimethylamine N-oxide reductase;    Twin arginine signal sequence;    Folded conformation;    Protein translocation;    Phospholipid;    Anaerobic growth;   

DOI  :  10.1016/S0014-5793(99)01661-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown