Difference between revisions of "Resistance against oxidative and electrophile stress"
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* 4.3.1. [[General stress proteins (controlled by SigB)]] | * 4.3.1. [[General stress proteins (controlled by SigB)]] | ||
* 4.3.2. [[Cell envelope stress proteins (controlled by SigM, V, W, X, Y)]] | * 4.3.2. [[Cell envelope stress proteins (controlled by SigM, V, W, X, Y)]] | ||
| − | * 4.3.3. [[Acid stress proteins (controlled by | + | * 4.3.3. [[Acid stress proteins (controlled by SigO-RsoA)]] |
* 4.3.4. [[Heat shock proteins]] | * 4.3.4. [[Heat shock proteins]] | ||
* 4.3.5. [[Cold stress proteins]] | * 4.3.5. [[Cold stress proteins]] | ||
| Line 25: | Line 25: | ||
* ''[[adhA]]'' | * ''[[adhA]]'' | ||
* ''[[adhR]]'' | * ''[[adhR]]'' | ||
| + | * ''[[ahpA]]'' | ||
* ''[[ahpC]]'' | * ''[[ahpC]]'' | ||
* ''[[ahpF]]'' | * ''[[ahpF]]'' | ||
| + | * ''[[ahpT]]'' | ||
* ''[[aldY]]'' | * ''[[aldY]]'' | ||
* ''[[azoR1]]'' | * ''[[azoR1]]'' | ||
| Line 40: | Line 42: | ||
* ''[[catE]]'' | * ''[[catE]]'' | ||
* ''[[catR]]'' | * ''[[catR]]'' | ||
| + | * ''[[cotJC]]'' | ||
* ''[[csbA]]'' | * ''[[csbA]]'' | ||
* ''[[csbB]]'' | * ''[[csbB]]'' | ||
| Line 49: | Line 52: | ||
* ''[[glxB]]'' | * ''[[glxB]]'' | ||
* ''[[guaD]]'' | * ''[[guaD]]'' | ||
| + | * ''[[hpf]]'' | ||
* ''[[hxlA]]'' | * ''[[hxlA]]'' | ||
* ''[[hxlB]]'' | * ''[[hxlB]]'' | ||
| Line 103: | Line 107: | ||
* ''[[yjbC]]'' | * ''[[yjbC]]'' | ||
* ''[[yjgD]]'' | * ''[[yjgD]]'' | ||
| − | |||
* ''[[ylxP]]'' | * ''[[ylxP]]'' | ||
* ''[[ymaD]]'' | * ''[[ymaD]]'' | ||
| Line 116: | Line 119: | ||
* ''[[yugU]]'' | * ''[[yugU]]'' | ||
* ''[[yvgN]]'' | * ''[[yvgN]]'' | ||
| − | |||
* ''[[ywiE]]'' | * ''[[ywiE]]'' | ||
Latest revision as of 17:36, 31 May 2016
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Contents
Genes in this functional category
- aag
- adhA
- adhR
- ahpA
- ahpC
- ahpF
- ahpT
- aldY
- azoR1
- azoR2
- brxA
- brxB
- bsaA
- bshA
- bshB1
- bshB2
- bshC
- catD
- catE
- catR
- cotJC
- csbA
- csbB
- csbC
- cypC
- dps
- efeB
- glxA
- glxB
- guaD
- hpf
- 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
- ylxP
- ymaD
- yodB
- yodC
- yojM
- yqhB
- yqjL
- yqjM
- yraA
- ytpQ
- yugU
- yvgN
Additional candidates (based on similarity)
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)
