Difference between revisions of "MrgA"
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+ | ==Original publications== | ||
<pubmed>9393687,14563870,7667267,12486061,8396117,9393707,8709848,8932315,,11532148, </pubmed> | <pubmed>9393687,14563870,7667267,12486061,8396117,9393707,8709848,8932315,,11532148, </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:04, 23 January 2010
- 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,
|
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
|
Contents
The gene
Basic information
- Locus tag: BSU32990
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 2CHP
- UniProt: P37960
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: mrgA PubMed
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
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)