Difference between revisions of "OhrR"

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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU13150 ohrR]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU13150 ohrR]
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=OhrR OhrR]
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 16 kDa, 6.364   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 16 kDa, 6.364   
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13150&redirect=T BSU13150]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ykmA.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ykmA.html]
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
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* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:'''  
 
* '''Modification:'''  
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** S-bacillithiolated by NaOCl and CHP stress on Cys-15, this results in release from the'' [[ohrA]]'' promoter {{PubMed|21749987}}  
 
** S-bacillithiolated by NaOCl and CHP stress on Cys-15, this results in release from the'' [[ohrA]]'' promoter {{PubMed|21749987}}  
  
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* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
 
** forms dimers
 
** forms dimers
 +
** [[BrxA]]-[[OhrR]], to de-bacillithiolate S-bacillithiolated [[OhrR]] {{PubMed|24313874}}
 +
** [[BrxB]]-[[OhrR]], to de-bacillithiolate S-bacillithiolated [[OhrR]] {{PubMed|24313874}}
  
 
* '''[[Localization]]:''' cytoplasm (according to Swiss-Prot)
 
* '''[[Localization]]:''' cytoplasm (according to Swiss-Prot)
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU13150&redirect=T BSU13150]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1Z91 1Z91] (reduced form),  [http://www.rcsb.org/pdb/explore.do?structureId=1Z9C 1Z9C] (complex with ''[[ohrA]]'' promoter)
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1Z91 1Z91] (reduced form),  [http://www.rcsb.org/pdb/explore.do?structureId=1Z9C 1Z9C] (complex with ''[[ohrA]]'' promoter)
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ohrR_1381434_1381877_-1 ohrR] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ohrR_1381434_1381877_-1 ohrR] {{PubMed|22383849}}
  
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* '''Sigma factor:''' [[SigA]]  
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* '''[[Sigma factor]]:''' [[SigA]]  
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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* '''Additional information:'''
 
* '''Additional information:'''
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** number of protein molecules per cell (minimal medium with glucose and ammonium): 133 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =
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=References=
 
=References=
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==Reviews==
 
==Reviews==
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<pubmed>22797754 </pubmed>
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<pubmed>22797754 20626317 19575568  20094649 25852656</pubmed>
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Antelmann H, Helmann JD.
 
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Thiol-based redox switches and gene regulation.
 
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Antioxid Redox Signal. 2011,14:1049-63.
 
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{{PubMed|20626317}}
 
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<pubmed>19575568  20094649 </pubmed>
 
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==Original Publications==
 
==Original Publications==
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<pubmed>21749987,16209951,18487332,17660290,17502599,12486061,11418552,18586944,11983871,18363800,19129220 9696771 21749987 22797754 </pubmed>
+
<pubmed>21749987,16209951,18487332,17660290,17502599,12486061,11418552,18586944,11983871,18363800,19129220 9696771 21749987 22797754 24313874 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Latest revision as of 11:02, 10 April 2015

  • 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
YkmA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
OhrR expression.png
















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

The protein

Basic information/ Evolution

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

Extended information on the protein

  • Kinetic information:
  • 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
  • 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:
    • 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

Your additional remarks

References

Reviews

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)

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