Chaperones involved in assembly and export of N-oxide reductases.
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.
Hatzixanthis
K
K
School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, England, UK.
Richardson
D J
DJ
Sargent
F
F
D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism / Q000502:physiology*; D010088:Oxidoreductases / Q000378:metabolism*; D010089:Oxidoreductases, N-Demethylating / Q000378:metabolism; D011485:Protein Binding; D021381:Protein Transport
D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D018832:Molecular Chaperones; C088083:TorD protein, E coli; C408585:twin-arginine translocase complex, E coli; D003577:Cytochrome P-450 Enzyme System; D010088:Oxidoreductases; D010089:Oxidoreductases, N-Demethylating; C023186:trimethylamine dehydrogenase; C431671:tertiary amine N-oxide reductase