The CydDC Family of Transporters and Their Roles in Oxidase Assembly and Homeostasis

Holyoake, Louise V and Poole, Robert K and Shepherd, Mark (2015) The CydDC Family of Transporters and Their Roles in Oxidase Assembly and Homeostasis. Advances in Microbial Physiology, 66 . pp. 1-53. ISSN 0065-2911. (doi:https://doi.org/10.1016/bs.ampbs.2015.04.002) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://www.dx.doi.org/10.1016/bs.ampbs.2015.04.002

Abstract

The CydDC complex of Escherichia coli is a heterodimeric ATP-binding cassette type transporter (ABC transporter) that exports the thiol-containing redox-active molecules cysteine and glutathione. These reductants are thought to aid redox homeostasis of the periplasm, permitting correct disulphide folding of periplasmic and secreted proteins. Loss of CydDC results in the periplasm becoming more oxidising and abolishes the assembly of functional bd-type respiratory oxidases that couple the oxidation of ubiquinol to the reduction of oxygen to water. In addition, CydDC-mediated redox control is important for haem ligation during cytochrome c assembly. Given the diverse roles for CydDC in redox homeostasis, respiratory metabolism and the maturation of virulence factors, this ABC transporter is an intriguing system for researchers interested in both the physiology of redox perturbations and the role of low-molecular-weight thiols during infection.

Item Type: Article
Subjects: Q Science > QR Microbiology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Mark Shepherd
Date Deposited: 12 Aug 2015 12:00 UTC
Last Modified: 13 Aug 2015 08:31 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/50177 (The current URI for this page, for reference purposes)
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