Resistance against oxidative and electrophile stress

Parent categories	4. Lifestyles 4.3. Coping with stress
Neighbouring categories	4.3.1. General stress proteins (controlled by SigB) 4.3.2. Cell envelope stress proteins (controlled by SigM, V, W, X, Y) 4.3.3. Acid stress proteins (controlled by SigO-RsoA) 4.3.4. Heat shock proteins 4.3.5. Cold stress proteins 4.3.6. Coping with hyper-osmotic stress 4.3.7. Coping with hypo-osmotic stress 4.3.8. Resistance against oxidative and electrophile stress 4.3.9. Resistance against other toxic compounds (nitric oxide, phenolic acids, flavonoids, oxalate) 4.3.10. Resistance against toxic metals 4.3.11. Resistance against toxins/ antibiotics 4.3.12. Biosynthesis of antibacterial compounds 4.3.13. Toxins, antitoxins and immunity against toxins
Related categories	none
Overview on the categories (Excel file) All genes and their categories (Excel file)

Genes in this functional category

• aag
• adhA
• adhR
• ahpC
• ahpF
• aldY
• azoR1
• azoR2
• brxA
• brxB
• bsaA
• bshA
• bshB1
• bshB2
• bshC
• catD
• catE
• catR
• csbA
• csbB
• csbC
• cypC
• dps
• efeB
• glxA
• glxB
• guaD
• hxlA
• hxlB
• hxlR
• hypO
• hypR
• katA
• katE
• katX
• liaF
• liaG
• liaH
• liaI
• liaR
• liaS
• mgsR
• mhqA
• mhqD
• mhqE
• mhqN
• mhqO
• mhqP
• mhqR
• mrgA
• msrA
• msrB
• nfrA
• ohrA
• ohrB
• ohrR
• perR
• rnr
• sodA
• sodF
• spx
• sqhC
• tpx
• trxA
• trxB
• ydaG
• ydeA
• ydhK
• yerD
• yfhE
• yfiT
• yfkH
• yfkI
• yfkJ
• yfkM
• yfkS
• yflA
• yhdN
• yitT
• yjbC
• yjgD
• ykuV
• ylxP
• ymaD
• yodB
• yodC
• yojM
• yqhB
• yqjL
• yqjM
• yraA
• ytpQ
• yugU
• yvgN
• yvyD

• ywiE
• yxiS
• yxjJ

Additional candidates (based on similarity)

• ydbD
• ydhU/1
• ygaF
• yjqC

Important original publications

Alexander Reder, Dirk Höper, Ulf Gerth, Michael Hecker
Contributions of individual σB-dependent general stress genes to oxidative stress resistance of Bacillus subtilis.
J Bacteriol: 2012, 194(14);3601-10
[PubMed:22582280] [WorldCat.org] [DOI] (I p)

Reviews

Vu Van Loi, Martina Rossius, Haike Antelmann
Redox regulation by reversible protein S-thiolation in bacteria.
Front Microbiol: 2015, 6;187
[PubMed:25852656] [WorldCat.org] [DOI] (P e)

Jun Lu, Arne Holmgren
The thioredoxin antioxidant system.
Free Radic Biol Med: 2014, 66;75-87
[PubMed:23899494] [WorldCat.org] [DOI] (I p)

James M Dubbs, Skorn Mongkolsuk
Peroxide-sensing transcriptional regulators in bacteria.
J Bacteriol: 2012, 194(20);5495-503
[PubMed:22797754] [WorldCat.org] [DOI] (I p)

Maarten Mols, Tjakko Abee
Primary and secondary oxidative stress in Bacillus.
Environ Microbiol: 2011, 13(6);1387-94
[PubMed:21352461] [WorldCat.org] [DOI] (I p)

Peter Zuber
Management of oxidative stress in Bacillus.
Annu Rev Microbiol: 2009, 63;575-97
[PubMed:19575568] [WorldCat.org] [DOI] (I p)

Haike Antelmann, Michael Hecker, Peter Zuber
Proteomic signatures uncover thiol-specific electrophile resistance mechanisms in Bacillus subtilis.
Expert Rev Proteomics: 2008, 5(1);77-90
[PubMed:18282125] [WorldCat.org] [DOI] (I p)

B C Dowds
The oxidative stress response in Bacillus subtilis.
FEMS Microbiol Lett: 1994, 124(3);255-63
[PubMed:7851732] [WorldCat.org] [DOI] (P p)