Unraveling the functions of unusual thioredoxins : the stories of CnoX and CcTrx1
(2018)
Files
Thesis_Final.pdf
Restricted Access - Adobe PDF
- 32.91 MB
Details
- Authors
- Supervisors
- Collet, Jean-François
- Abstract
- Thioredoxins are a highly-conserved family of proteins. They are present in all organisms where they perform a variety of functions, often related to redox homeostasis. During my thesis, I studied two proteins belonging to this family, CcTrx1 and CnoX. I demonstrated that, in the model bacterium Caulobacter crescentus, CcTrx1 was a classical reductase but that its complex regulation was critical for cell cycle progression. I also discovered the function of CnoX, a unique protein that combines redox and chaperone functions. In Escherichia coli, CnoX is activated by HOCl and protects its substrates from over-oxidation and aggregation, before transferring them to cytoplasmic foldases. In C. crescentus, CnoX is both a reductase and a chaperone.
- Affiliations
Citations
Goemans, C. (2018). Unraveling the functions of unusual thioredoxins : the stories of CnoX and CcTrx1. https://hdl.handle.net/2078.5/39209