Chaperones involved in assembly and export of N-oxide reductases

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

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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
Faculty \ School:	Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
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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