Hatzixanthis, K., Richardson, D.J. ORCID: https://orcid.org/0000-0002-6847-1832 and Sargent, F.
(2005)
Chaperones involved in assembly and export of N-oxide reductases.
Biochemical Society Transactions, 33 (1).
pp. 124-126.
ISSN 1470-8752
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.
Item Type: | Article |
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Faculty \ School: | Faculty of Science > School of Biological Sciences |
Depositing User: | EPrints Services |
Date Deposited: | 01 Oct 2010 13:37 |
Last Modified: | 17 May 2023 00:01 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/977 |
DOI: | 10.1042/BST0330124 |
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