Chaperones involved in assembly and export of N-oxide reductases. (1st February 2005)

• Record Type: Journal Article
• Authors: Hatzixanthis, K.; Richardson, D.J.; Sargent, F.
• Is Part Of: Biochemical Society transactions. Volume 33:Number 1(2005)
• Page Start: 124
• Page End: 126
• Publication Date: 2005-02-01
• Subjects: molecular chaperone -- molybdopterin cofactor -- protein–protein interactions -- Tat protein transport system -- trimethylamine N-oxide (TMAO) reductase -- twin-arginine signal peptide; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0330124
• Languages: English
• ISSNs: 0300-5127

Abstract

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.