MrgA

• Description: iron storage protein, DNA-binding stress protein, forms highly stable, multimeric protein-DNA complexes which protect against oxidative killing
  
  

Gene name	mrgA
Synonyms
Essential	no
Product	mini-ferritin, DNA-binding stress protein
Function	iron storage, protection against oxidative stress
Metabolic function and regulation of this protein in SubtiPathways: Stress
MW, pI	17 kDa, 4.597
Gene length, protein length	459 bp, 153 aa
Immediate neighbours	yusZ, htrB
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: BSU32990

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: forms highly stable, multimeric protein-DNA complexes which protect against oxidative killing

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

• Paralogous protein(s): Dps

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s): contains an iron-sulfur cluster

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 2CHP

• UniProt: P37960

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: mrgA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by hydrogen peroxide (PerR) PubMed

• Regulatory mechanism:
  • PerR: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Emilia Chiancone, Pierpaolo Ceci, Andrea Ilari, Frederica Ribacchi, Simonetta Stefanini
Iron and proteins for iron storage and detoxification.
Biometals: 2004, 17(3);197-202
[PubMed:15222465] [WorldCat.org] [DOI] (P p)

Original publications

Mayuree Fuangthong, John D Helmann
Recognition of DNA by three ferric uptake regulator (Fur) homologs in Bacillus subtilis.
J Bacteriol: 2003, 185(21);6348-57
[PubMed:14563870] [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)

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)

L Casillas-Martinez, P Setlow
Alkyl hydroperoxide reductase, catalase, MrgA, and superoxide dismutase are not involved in resistance of Bacillus subtilis spores to heat or oxidizing agents.
J Bacteriol: 1997, 179(23);7420-5
[PubMed:9393707] [WorldCat.org] [DOI] (P p)

H Antelmann, S Engelmann, R Schmid, A Sorokin, A Lapidus, M Hecker
Expression of a stress- and starvation-induced dps/pexB-homologous gene is controlled by the alternative sigma factor sigmaB in Bacillus subtilis.
J Bacteriol: 1997, 179(23);7251-6
[PubMed:9393687] [WorldCat.org] [DOI] (P p)

N Bsat, L Chen, J D Helmann
Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes.
J Bacteriol: 1996, 178(22);6579-86
[PubMed:8932315] [WorldCat.org] [DOI] (P p)

L Chen, J D Helmann
Bacillus subtilis MrgA is a Dps(PexB) homologue: evidence for metalloregulation of an oxidative-stress gene.
Mol Microbiol: 1995, 18(2);295-300
[PubMed:8709848] [WorldCat.org] [DOI] (P p)

L Chen, L Keramati, J D Helmann
Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions.
Proc Natl Acad Sci U S A: 1995, 92(18);8190-4
[PubMed:7667267] [WorldCat.org] [DOI] (P p)

L Chen, L P James, J D Helmann
Metalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially repressed by metal ions.
J Bacteriol: 1993, 175(17);5428-37
[PubMed:8396117] [WorldCat.org] [DOI] (P p)