How bacterial thioredoxin proteins make or break disulfides
(2016)
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- Authors
- Supervisors
- Collet, Jean-François
- Abstract
- Thioredoxin-fold proteins are ubiquitous and carry out a variety of functions, mostly thiol-disulfide exchange reactions. During my thesis, I studied proteins involved either in the formation or in the reduction of disulfide bonds in bacteria. I first unravelled the oxidative protein folding system of Pseudomonas aeruginosa. This study led to the discovery of two membrane proteins uniquely delivering disulfide bonds to a soluble oxidoreductase, which in turn oxidizes secreted proteins, including virulence factors. Disruption of this machinery dramatically decreases P. aeruginosa virulence, opening the way to the design of novel anti-bacterial molecules. Second, I characterized the redox interactome of Escherichia coli Trx1. This study led to the identification of more than 200 new Trx1 targets, involved in a variety of cellular processes, allowing me to fully grasp the importance of Trx1 in controlling the redox state of intracellular proteins.
- Affiliations
Citations
Arts, I. (2016). How bacterial thioredoxin proteins make or break disulfides. https://hdl.handle.net/2078.5/179756