TY - JOUR
T1 - Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S-Bacillithiolated OhrR and MetE
AU - Gaballa, Ahmed
AU - Chi, Bui Khanh
AU - Roberts, Alexandra A.
AU - Becher, Dörte
AU - Hamilton, Christopher
AU - Antelmann, Haike
AU - Helmann, John D.
PY - 2014/7/20
Y1 - 2014/7/20
N2 - 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.
AB - 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.
U2 - 10.1089/ars.2013.5327
DO - 10.1089/ars.2013.5327
M3 - Article
VL - 21
SP - 357
EP - 367
JO - Antioxidants & Redox Signaling
JF - Antioxidants & Redox Signaling
SN - 1523-0864
IS - 3
ER -