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In bacillithiol (BSH)-utilizing organisms, protein S-bacillithiolation functions as a redox switch in response to oxidative stress and protects critical Cys residues against overoxidation. In Bacillus subtilis, both the redox-sensing repressor OhrR and the methionine synthase MetE are redox controlled by S-bacillithiolation in vivo. Here, we identify pathways of protein de-bacillithiolation and test the hypothesis that YphP(BrxA) and YqiW(BrxB) act as bacilliredoxins (Brx) to remove BSH from OhrR and MetE mixed disulfides.

antioxidants and redox signaling

Redox Regulation in <i>Bacillus subtilis</i>: The Bacilliredoxins BrxA(YphP) and BrxB(YqiW) Function in De-Bacillithiolation of <i>S</i>-Bacillithiolated OhrR and MetE

Redox Regulation in Bacillus subtilis: The Bacilliredoxins BrxA(YphP) and BrxB(YqiW) Function in De-Bacillithiolation of S-Bacillithiolated OhrR and MetE