OhrR

• Description: transcription repressor of the ohrA gene
  
  

Gene name	ohrR
Synonyms	ykmA
Essential	no
Product	transcription repressor (MarR family)
Function	regulation of ohrA expression in response to organic peroxides
Gene expression levels in SubtiExpress: ohrR
Interactions involving this protein in SubtInteract: OhrR
MW, pI	16 kDa, 6.364
Gene length, protein length	441 bp, 147 aa
Immediate neighbours	ohrA, ohrB
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

transcription factors and their control, resistance against oxidative and electrophile stress

The OhrR regulon:

• ohrA

The gene

Basic information

• Locus tag: BSU13150

Database entries

• BsubCyc: BSU13150

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: MarR family

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • senses organic peroxides and NaOCl, released from DNA upon oxidation of an active site cysteine
  • S-bacillithiolated by NaOCl and CHP stress on Cys-15, this results in release from the ohrA promoter PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • forms dimers
  • BrxA-OhrR, to de-bacillithiolate S-bacillithiolated OhrR PubMed
  • BrxB-OhrR, to de-bacillithiolate S-bacillithiolated OhrR PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU13150

• Structure: 1Z91 (reduced form), 1Z9C (complex with ohrA promoter)

• UniProt: O34777

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ohrR PubMed

• Expression browser: ohrR PubMed

• Sigma factor: SigA

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 133 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

John Helmann, Cornell University, USA Homepage

Richard Brennan, Houston, Texas, USA Homepage

References

Original Publications

Ahmed Gaballa, Bui Khanh Chi, Alexandra A Roberts, Dörte Becher, Chris J Hamilton, Haike Antelmann, John D Helmann
Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and MetE.
Antioxid Redox Signal: 2014, 21(3);357-67
[PubMed:24313874] [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)

Bui Khanh Chi, Katrin Gronau, Ulrike Mäder, Bernd Hessling, Dörte Becher, Haike Antelmann
S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics.
Mol Cell Proteomics: 2011, 10(11);M111.009506
[PubMed:21749987] [WorldCat.org] [DOI] (I p)

Warawan Eiamphungporn, Sumarin Soonsanga, Jin-Won Lee, John D Helmann
Oxidation of a single active site suffices for the functional inactivation of the dimeric Bacillus subtilis OhrR repressor in vitro.
Nucleic Acids Res: 2009, 37(4);1174-81
[PubMed:19129220] [WorldCat.org] [DOI] (I p)

Sumarin Soonsanga, Jin-Won Lee, John D Helmann
Conversion of Bacillus subtilis OhrR from a 1-Cys to a 2-Cys peroxide sensor.
J Bacteriol: 2008, 190(17);5738-45
[PubMed:18586944] [WorldCat.org] [DOI] (I p)

Falko Hochgräfe, Carmen Wolf, Stephan Fuchs, Manuel Liebeke, Michael Lalk, Susanne Engelmann, Michael Hecker
Nitric oxide stress induces different responses but mediates comparable protein thiol protection in Bacillus subtilis and Staphylococcus aureus.
J Bacteriol: 2008, 190(14);4997-5008
[PubMed:18487332] [WorldCat.org] [DOI] (I p)

Sumarin Soonsanga, Jin-Won Lee, John D Helmann
Oxidant-dependent switching between reversible and sacrificial oxidation pathways for Bacillus subtilis OhrR.
Mol Microbiol: 2008, 68(4);978-86
[PubMed:18363800] [WorldCat.org] [DOI] (I p)

Sumarin Soonsanga, Mayuree Fuangthong, John D Helmann
Mutational analysis of active site residues essential for sensing of organic hydroperoxides by Bacillus subtilis OhrR.
J Bacteriol: 2007, 189(19);7069-76
[PubMed:17660290] [WorldCat.org] [DOI] (P p)

Jin-Won Lee, Sumarin Soonsanga, John D Helmann
A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR.
Proc Natl Acad Sci U S A: 2007, 104(21);8743-8
[PubMed:17502599] [WorldCat.org] [DOI] (P p)

Minsun Hong, Mayuree Fuangthong, John D Helmann, Richard G Brennan
Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family.
Mol Cell: 2005, 20(1);131-41
[PubMed:16209951] [WorldCat.org] [DOI] (P p)

John D Helmann, Ming Fang Winston Wu, Ahmed Gaballa, Phil A Kobel, Maud M Morshedi, Paul Fawcett, Chris Paddon
The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors.
J Bacteriol: 2003, 185(1);243-53
[PubMed:12486061] [WorldCat.org] [DOI] (P p)

Mayuree Fuangthong, John D Helmann
The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative.
Proc Natl Acad Sci U S A: 2002, 99(10);6690-5
[PubMed:11983871] [WorldCat.org] [DOI] (P p)

M Fuangthong, S Atichartpongkul, S Mongkolsuk, J D Helmann
OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis.
J Bacteriol: 2001, 183(14);4134-41
[PubMed:11418552] [WorldCat.org] [DOI] (P p)

U Völker, K K Andersen, H Antelmann, K M Devine, M Hecker
One of two osmC homologs in Bacillus subtilis is part of the sigmaB-dependent general stress regulon.
J Bacteriol: 1998, 180(16);4212-8
[PubMed:9696771] [WorldCat.org] [DOI] (P p)