Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 357-367 |
| Number of pages | 11 |
| Journal | Antioxidants & Redox Signaling |
| Volume | 21 |
| Issue number | 3 |
| Early online date | 13 Mar 2014 |
| DOIs | |
| Publication status | Published - 20 Jul 2014 |
Profiles
-
Christopher Hamilton
- School of Chemistry, Pharmacy and Pharmacology - Associate Professor
- Synthetic and Medicinal Chemistry - Member
Person: Research Group Member, Academic, Teaching and Research
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