Difference between revisions of "HypR"
| Line 89: | Line 89: | ||
* '''Structure:''' | * '''Structure:''' | ||
| − | + | reduced HypRC14S dimer [http://www.pdb.org/pdb/explore.do?structureId=4A5N] | |
| − | + | oxidized HypR C14-C49' intersubunit disulfide-linked dimer [http://www.pdb.org/pdb/explore.do?structureId=4A5M] | |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37486 P37486] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P37486 P37486] | ||
| Line 136: | Line 136: | ||
=Original articles= | =Original articles= | ||
| − | <pubmed>22238377</pubmed> | + | <pubmed>22238377</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 09:13, 13 January 2012
- Description: MarR/DUF24-family transcription regulator, positively controls the nitroreductase gene yfkO (hypO) in response to disulfide stress
| Gene name | yybR (hypR) |
| Synonyms | hypR |
| Essential | no |
| Product | MarR/DUF24-family transcription regulator HypR |
| Function | positively controls nitroreductase gene yfkO (hypO) in response to disulfide stress (diamide, NaOCl) |
| MW, pI | 14 kDa, 8.415 |
| Gene length, protein length | 375 bp, 125 aa |
| Immediate neighbours | cotF, ppaC |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Contents
- 1 Categories containing this gene/protein
- 2 This gene is a member of the following regulons
- 3 This gene is a member of the following regulons
- 4 The YybR (HypR) regulon:
- 5 The gene
- 6 The protein
- 7 Expression and regulation
- 8 Biological materials
- 9 Labs working on this gene/protein
- 10 Your additional remarks
- 11 References
- 12 Original articles
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
This gene is a member of the following regulons
The YybR (HypR) regulon:
The gene
Basic information
- Locus tag: BSU40540
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
hypR autoregulated by disulfide stress
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: MarR/DUF24-family regulator
- Paralogous protein(s): YdeP,YkvN
Extended information on the protein
- Kinetic information: Cys14 redox sensing Cys, has lower pKa of 6.36 PubMed
- Domains: 5 alpha helices, 2 beta sheets, MarR-fold with wHTH motif, alpha4 major groove recognition helix, beta2 and 3 form the wing; alpha5 dimer interface PubMed
- Modification: oxidized to Cys14-Cys49' intersubunit disulfides by disulfide stress PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasmic
Database entries
- Structure:
reduced HypRC14S dimer [3] oxidized HypR C14-C49' intersubunit disulfide-linked dimer [4]
- UniProt: P37486
- KEGG entry: [5]
- E.C. number:
Additional information
Expression and regulation
- Operon: yybR (hypR)(according to DBTBS)
- Regulation: activated by disulfide stress conditions (diamide, NaOCl) in vivo and in vitro PubMed
- Regulatory mechanism: redox-controlled by Cys14-Cys49' intersubunit disulfide formation by diamide and NaOCl in vitro and vivo PubMed
- Additional information: Cys14 and Cys49' are about 8-9 Angstroem apart in reduced HypR-Dimer, oxidation moves the major groove recognition alpha4 helices of the HypR dimer about 4 Angstroem towards each other that leads to activation of HypR PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Haike Antelmann,University of Greifswald, Germany
Your additional remarks
References
Original articles
Gottfried J Palm, Bui Khanh Chi, Paul Waack, Katrin Gronau, Dörte Becher, Dirk Albrecht, Winfried Hinrichs, Randy J Read, Haike Antelmann
Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR.
Nucleic Acids Res: 2012, 40(9);4178-92
[PubMed:22238377]
[WorldCat.org]
[DOI]
(I p)
