PerR

• Description: transcriptional repressor of the peroxide regulon
  
  

Gene name	perR
Synonyms	ygaG
Essential	no
Product	transcriptional repressor
Function	regulation of the response to peroxide
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 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

PerR regulon

The gene

Basic information

• Locus tag: BSU08730

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: Fur family (according to Swiss-Prot)

• Paralogous protein(s): Zur, Fur

Genes repressed by PerR

ahpC-ahpF PubMed, zosA

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 iron-sulfur cluster

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 2RGV 3F8N

• UniProt: P71086

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: perR PubMed

• Sigma factor: SigA PubMed

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

• Regulatory mechanism:
  • PerR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant: HB0509 (spc), available in John Helmann's and Jörg Stülke's labs, also GP868 (fur::mls, perR::spc).

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

John Helmann, Cornell University, USA Homepage

References

Reviews

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

PubMed