Open AccessS-Bacillithiolation Protects Conserved and Essential Proteins Against Hypochlorite Stress inFirmicutesBacteria
Author(s) -
Bui Khanh,
A. W. Roberts,
Trần Thị Thanh Huyền,
Katrin Bäsell,
Dörte Becher,
Dirk Albrecht,
Chris J. Hamilton,
Haike Antelmann
Publication year - 2013
Publication title -
antioxidants and redox signaling
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.277
H-Index - 190
eISSN - 1557-7716
pISSN - 1523-0864
DOI - 10.1089/ars.2012.4686
Subject(s) - biochemistry , bacillus subtilis , biology , biosynthesis , hypothetical protein , thiamine pyrophosphate , amino acid , chemistry , cofactor , bacteria , enzyme , genetics , gene
Protein S-bacillithiolations are mixed disulfides between protein thiols and the bacillithiol (BSH) redox buffer that occur in response to NaOCl in Bacillus subtilis. We used BSH-specific immunoblots, shotgun liquid chromatography (LC)-tandem mass spectrometry (MS/MS) analysis and redox proteomics to characterize the S-bacillithiolomes of B. subtilis, B. megaterium, B. pumilus, B. amyloliquefaciens, and Staphylococcus carnosus and also measured the BSH/oxidized bacillithiol disulfide (BSSB) redox ratio after NaOCl stress.