Mavridou, D.A.I and Saridakis, E and Kritsiligkou, P and Goddard, Alan and Stevens, J.M and Ferguson, S.J and Redfield, C (2011) Oxidation state-dependent protein-protein interactions in disulfide cascades. Journal of Biological Chemistry, 286 (28). pp. 24943-24956. ISSN 0021-9258

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Abstract

Bacterial growth and pathogenicity depend on the correct formation of disulfide bonds, a process controlled by the Dsb system in the periplasm of Gram-negative bacteria. Proteins with a thioredoxin fold play a central role in this process. A general feature of thiol-disulfide exchange reactions is the need to avoid a long lived product complex between protein partners. We use a multidisciplinary approach, involving NMR, x-ray crystallography, surface plasmon resonance, mutagenesis, and in vivo experiments, to investigate the interaction between the two soluble domains of the transmembrane reductant conductor DsbD. Our results show oxidation state-dependent affinities between these two domains. These observations have implications for the interactions of the ubiquitous thioredoxin-like proteins with their substrates, provide insight into the key role played by a unique redox partner with an immunoglobulin fold, and are of general importance for oxidative protein-folding pathways in all organisms.

Item Type:	Article
Keywords:	DsbD
Subjects:	C Biological Sciences > C700 Molecular Biology, Biophysics and Biochemistry
Divisions:	College of Sciences > Faculty of Science > School of Life Sciences
Depositing User:	Alan Goddard
Date Deposited:	16 Nov 2012 11:51
Last Modified:	08 May 2013 15:23
URI:	http://eprints.lincoln.ac.uk/id/eprint/6843

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