Banaś, Anna Marta Bocian-Ostrzycka, Katarzyna Marta Plichta, Maciej Dunin-Horkawicz, Stanisław Ludwiczak, Jan Płaczkiewicz, Jagoda Jagusztyn-Krynicka, Elżbieta Katarzyna C8J_1298, a bifunctional thiol oxidoreductase of <i>Campylobacter jejuni</i>, affects Dsb (disulfide bond) network functioning <div><p>Posttranslational generation of disulfide bonds catalyzed by bacterial Dsb (disulfide bond) enzymes is essential for the oxidative folding of many proteins. Although we now have a good understanding of the <i>Escherichia coli</i> disulfide bond formation system, there are significant gaps in our knowledge concerning the Dsb systems of other bacteria, including <i>Campylobacter jejuni</i>, a food-borne, zoonotic pathogen. We attempted to gain a more complete understanding of the process by thorough analysis of C8J_1298 functioning <i>in vitro</i> and <i>in vivo</i>. C8J_1298 is a homodimeric thiol-oxidoreductase present in wild type (<i>wt</i>) cells, in both reduced and oxidized forms. The protein was previously described as a homolog of DsbC, and thus potentially should be active in rearrangement of disulfides. Indeed, biochemical studies with purified protein revealed that C8J_1298 shares many properties with EcDsbC. However, its activity <i>in vivo</i> is dependent on the genetic background, namely, the set of other Dsb proteins present in the periplasm that determine the redox conditions. In <i>wt C</i>. <i>jejuni</i> cells, C8J_1298 potentially works as a DsbG involved in the control of the cysteine sulfenylation level and protecting single cysteine residues from oxidation to sulfenic acid. A strain lacking only C8J_1298 is indistinguishable from the wild type strain by several assays recognized as the criteria to determine isomerization or oxidative Dsb pathways. Remarkably, in C. <i>jejuni</i> strain lacking DsbA1, the protein involved in generation of disulfides, C8J_1298 acts as an oxidase, similar to the homodimeric oxidoreductase of <i>Helicobater pylori</i>, HP0231. In <i>E</i>. <i>coli</i>, C8J_1298 acts as a bifunctional protein, also resembling HP0231. These findings are strongly supported by phylogenetic data. We also showed that CjDsbD (C8J_0565) is a C8J_1298 redox partner.</p></div> bifunctional thiol oxidoreductase;disulfide bond;Campylobacter jejuni;C 8J acts;oxidative Dsb pathways;Escherichia coli disulfide bond formation system;C 8J;HP 0231.;C 8J redox partner;cysteine sulfenylation level;protein;C 8J shares 2020-03-23
    https://plos.figshare.com/articles/dataset/C8J_1298_a_bifunctional_thiol_oxidoreductase_of_i_Campylobacter_jejuni_i_affects_Dsb_disulfide_bond_network_functioning/12019275
10.1371/journal.pone.0230366