Difference between revisions of "PerR"

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(Original Publications)
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==Original Publications==
 
==Original Publications==
'''Addititonal publications:''' {{PubMed|23057863}}
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<pubmed> 8932315,18487332,14563870, 16766519,17158660,12486061,11532148,12180919,16166527, 15231799, 12029044,10913706, 21398634, 9701813, 16541078, 12029044, ,11532148, 12029044, 19508285 , 22194458 23645680 23057863</pubmed>
<pubmed> 8932315,18487332,14563870, 16766519,17158660,12486061,11532148,12180919,16166527, 15231799, 12029044,10913706, 21398634, 9701813, 16541078, 12029044, ,11532148, 12029044, 19508285 , 22194458 </pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:35, 7 May 2013

  • Description: transcriptional repressor of the peroxide regulon

Gene name perR
Synonyms ygaG
Essential no
Product transcriptional repressor (Fur family)
Function regulation of the response to peroxide
Gene expression levels in SubtiExpress: perR
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 16 kDa, 5.888
Gene length, protein length 435 bp, 145 aa
Immediate neighbours ygaF, ygzB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PerR context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PerR 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

PerR regulon

The PerR regulon

The gene

Basic information

  • Locus tag: BSU08730

Phenotypes of a mutant

  • resistant to hydrogen peroxide, accumulates a porphyrin-like compound, and grows very slowly (due to heme sequestration by KatA) PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

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

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • selective metal catalyzed oxidation of two histidine residues of the regulatory site results in induction (loss of DNA-binding activity) PubMed
  • Cofactor(s): contains an Fe(2+) at the regulatory site and Zn(2+) PubMed
  • Effectors of protein activity:
    • responds to the presence of hydrogen peroxide

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • negative autoregulation PubMed
    • induced in the presence of hydrogen peroxide (PerR) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

John Helmann, Cornell University, USA Homepage

Your additional remarks

References

Reviews

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)

Melinda J Faulkner, John D Helmann
Peroxide stress elicits adaptive changes in bacterial metal ion homeostasis.
Antioxid Redox Signal: 2011, 15(1);175-89
[PubMed:20977351] [WorldCat.org] [DOI] (I p)

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)

David P Giedroc
Hydrogen peroxide sensing in Bacillus subtilis: it is all about the (metallo)regulator.
Mol Microbiol: 2009, 73(1);1-4
[PubMed:19508286] [WorldCat.org] [DOI] (I p)


Original Publications