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. 2018 Apr 20;293(16):5806-5807.
doi: 10.1074/jbc.H118.002699.

Stress control for a well-structured life

David C Goldstone  1 , Edward N Baker  2
Affiliations

Stress control for a well-structured life

David C Goldstone et al. J Biol Chem. .

Abstract

Aerobic life brings with it a need to respond to external redox stress in ways that preserve key processes. Suppressor of copper sensitivity (Scs) proteins contribute to this response in some bacteria, but have poorly defined molecular functions. Furlong et al. now demonstrate that two Scs proteins from Proteus mirabilis provide a redox relay functionally equivalent to, but structurally distinct from, the Dsb proteins that orchestrate disulfide bonding in Escherichia coli, emphasizing the wide prevalence of this mechanism in bacteria.

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Conflict of interest statement

The authors declare that they have no conflicts of interest with the contents of this article.

Figures

Figure 1.
Figure 1.
Structural variability in redox relay proteins. A, the ScsBα domain, shown here, comprises two Ig-fold subdomains, in contrast to DsbDα, which has only one. Subdomain A contains the two redox-active cysteine residues (gold spheres). B, schematic depiction of the variation in the periplasmic domains attached to the electron transporters Rhodobacter capsulatus CcdA, E. coli DsbD, P. mirabilis ScsB, and M. tuberculosis DipZ.
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