Formation of disulphide bonds between cysteine residues is key for the stability and activity of a range of exported bacterial proteins. Disulphide bond formation occurs during the oxidative protein folding processes that are catalysed by the DSB protein family. In this article, Heras and colleagues review oxidative folding pathways inEscherichia coliK12 and other bacteria and their impact on pathogenesis.
- Begoña Heras
- Stephen R. Shouldice
- Jennifer L. Martin
