Difference between revisions of "OhrR"

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=== Additional information===
 
=== Additional information===
  
 
+
[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ohrR_1381434_1381877_-1 Expression]
 
 
  
 
=The protein=
 
=The protein=

Revision as of 08:23, 25 January 2012

  • 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
MW, pI 16 kDa, 6.364
Gene length, protein length 441 bp, 147 aa
Immediate neighbours ohrA, ohrB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YkmA context.gif
This image was kindly provided by SubtiList




Categories containing this gene/protein

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

This gene is a member of the following regulons

The OhrR regulon:

The gene

Basic information

  • Locus tag: BSU13150

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

Expression

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • senses organic peroxides, released from DNA upon oxidation of an active site cysteine
    • S-bacillithiolation upon hypochlorite stress on Cys-15, this results in release from the ohrA promoter PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1Z91 (reduced form), 1Z9C (complex with ohrA promoter)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

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

Your additional remarks

References

Reviews

Antelmann H, Helmann JD.
Thiol-based redox switches and gene regulation.
Antioxid Redox Signal. 2011,14:1049-63.
PubMed

Victor Duarte, Jean-Marc Latour
PerR vs OhrR: selective peroxide sensing in Bacillus subtilis.
Mol Biosyst: 2010, 6(2);316-23
[PubMed:20094649] [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)


Original Publications

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)