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.
|Number of pages||11|
|Journal||Antioxidants & Redox Signaling|
|Early online date||13 Mar 2014|
|Publication status||Published - 20 Jul 2014|
- School of Pharmacy - Associate Professor
Person: Academic, Teaching & Research