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

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):

• Effectors of protein activity:

• Interactions:

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 2RGV

• Swiss prot entry: P71086

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• Regulation: negative autoregulation PubMed
  • repressed in the absence of hydrogen peroxide (PerR) PubMed

• Regulatory mechanism: repressed by PerR PubMed
  • PerR: transcription repression PubMed

• 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

References

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)

L Jacquamet, D A K Traoré, J-L Ferrer, O Proux, D Testemale, J-L Hazemann, E Nazarenko, A El Ghazouani, C Caux-Thang, V Duarte, J-M Latour
Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding.
Mol Microbiol: 2009, 73(1);20-31
[PubMed:19508285] [WorldCat.org] [DOI] (I p)

Mayuree Fuangthong, Andrew F Herbig, Nada Bsat, John D Helmann
Regulation of the Bacillus subtilis fur and perR genes by PerR: not all members of the PerR regulon are peroxide inducible.
J Bacteriol: 2002, 184(12);3276-86
[PubMed:12029044] [WorldCat.org] [DOI] (P p)

A F Herbig, J D Helmann
Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA.
Mol Microbiol: 2001, 41(4);849-59
[PubMed:11532148] [WorldCat.org] [DOI] (P p)

PubMed