The Scs disulfide reductase system cooperates with the metallochaperone CueP in Salmonella copper resistance.

ABSTRACT: The human pathogen Salmonella enterica serovar Typhimurium (S Typhimurium) contains a complex disulfide bond (Dsb) catalytic machinery. This machinery encompasses multiple Dsb thiol-disulfide oxidoreductases that mediate oxidative protein folding and a less-characterized suppressor of copper sensitivity (scs) gene cluster, associated with increased tolerance to copper. To better understand the function of the Salmonella Scs system, here we characterized two of its key components, the membrane protein ScsB and the periplasmic protein ScsC. Our results revealed that these two proteins form a redox pair in which the electron transfer from the periplasmic domain of ScsB (n-ScsB) to ScsC is thermodynamically driven. We also demonstrate that the Scs reducing pathway r

SUBMITTER: Subedi P 

PROVIDER: S-EPMC6827279 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature