PMID:15667282

Citation	Hatzixanthis, K, Richardson, DJ and Sargent, F (2005) Chaperones involved in assembly and export of N-oxide reductases. Biochem. Soc. Trans. 33:124-6
Abstract	Controlled targeting and transport of redox enzymes to and across the bacterial cytoplasmic membrane is essential for bacterial respiration. A subset of bacterial redox enzymes is exported as folded proteins on the Tat (twin-arginine transport) pathway. Protein export is the point-of-no-return for passenger proteins on the Tat pathway and it is crucial that complex, cofactor-containing enzymes are fully assembled before export is attempted. Using the Escherichia coli trimethylamine N-oxide reductase system as a model, we discuss here the molecular processes governing assembly and export of Tat-dependent enzymes.
Links	PubMed Online version:10.1042/BST0330124
Keywords	Cytochrome P-450 Enzyme System/metabolism; Escherichia coli Proteins/metabolism; Membrane Transport Proteins/metabolism; Molecular Chaperones/metabolism; Molecular Chaperones/physiology; Oxidoreductases/metabolism; Oxidoreductases, N-Demethylating/metabolism; Protein Binding; Protein Transport
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