Difference between revisions of "HypR"
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| − | * '''Description:''' MarR/DUF24-family transcription regulator, positively controls the nitroreductase gene ''yfkO''(hypO) in response to disulfide stress <br/><br/> | + | * '''Description:''' MarR/DUF24-family transcription regulator, positively controls the nitroreductase gene ''[[yfkO]]'' (hypO) in response to disulfide stress <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
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===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
| − | + | ''' hypO ohrA double mutant more sensitive to NaOCl stress than ohrA single mutant | |
=== Database entries === | === Database entries === | ||
| Line 55: | Line 55: | ||
=== Additional information=== | === Additional information=== | ||
| − | + | ''' hypR autoregulated by disulfide stress | |
| Line 64: | Line 64: | ||
* '''Catalyzed reaction/ biological activity:''' | * '''Catalyzed reaction/ biological activity:''' | ||
| − | * '''Protein family:'''MarR/DUF24-family regulator | + | * '''Protein family:''' MarR/DUF24-family regulator |
| − | * '''Paralogous protein(s):'''YdeP,YkvN | + | * '''Paralogous protein(s):''' YdeP,YkvN |
=== Extended information on the protein === | === Extended information on the protein === | ||
| − | * '''Kinetic information:'''Cys14 redox sensing Cys, has lower pKa of 6.36 | + | * '''Kinetic information:''' Cys14 redox sensing Cys, has lower pKa of 6.36 |
| − | * '''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 | + | * '''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 |
| − | * '''Modification:'''oxidized to Cys14-Cys49' intersubunit disulfides by disulfide stress | + | * '''Modification:''' oxidized to Cys14-Cys49' intersubunit disulfides by disulfide stress |
* '''Cofactor(s):''' | * '''Cofactor(s):''' | ||
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* '''Interactions:''' | * '''Interactions:''' | ||
| − | * '''Localization:'''cytoplasmic | + | * '''Localization:''' cytoplasmic |
=== Database entries === | === Database entries === | ||
| − | * '''Structure:'''tba | + | * '''Structure:''' tba |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37486 P37486] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P37486 P37486] | ||
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=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' ''yybR''(hypR)(according to [http://dbtbs.hgc.jp/COG/prom/yybR.html DBTBS]) | + | * '''Operon:''' ''yybR'' (hypR)(according to [http://dbtbs.hgc.jp/COG/prom/yybR.html DBTBS]) |
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
| − | * '''Regulation:'''activated by disulfide stress conditions (diamide, NaOCl) in vivo and in vitro | + | * '''Regulation:''' activated by disulfide stress conditions (diamide, NaOCl) in vivo and in vitro |
| − | * '''Regulatory mechanism:'''redox-controlled by Cys14-Cys49' intersubunit disulfide formation by diamide and NaOCl in vitro and vivo | + | * '''Regulatory mechanism:''' redox-controlled by Cys14-Cys49' intersubunit disulfide formation by diamide and NaOCl in vitro and vivo |
| − | * '''Additional information:'''Cys14 and Cys49' are about 8-9 Angstroem apart in reduced HypR-Dimer, oxidation moves the major groove recognition alpha helices of the HypR dimer about 4 Angstroem towards each other | + | * '''Additional information:''' Cys14 and Cys49' are about 8-9 Angstroem apart in reduced HypR-Dimer, oxidation moves the major groove recognition alpha helices of the HypR dimer about 4 Angstroem towards each other |
=Biological materials = | =Biological materials = | ||
Revision as of 10:38, 26 December 2011
- 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 hypO (yfkO) 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
Categories containing this gene/protein
transcription factors and their control
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU40540
Phenotypes of a mutant
hypO ohrA double mutant more sensitive to NaOCl stress than ohrA single 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
- 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
- Modification: oxidized to Cys14-Cys49' intersubunit disulfides by disulfide stress
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasmic
Database entries
- Structure: tba
- UniProt: P37486
- KEGG entry: [3]
- 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
- Regulatory mechanism: redox-controlled by Cys14-Cys49' intersubunit disulfide formation by diamide and NaOCl in vitro and vivo
- Additional information: Cys14 and Cys49' are about 8-9 Angstroem apart in reduced HypR-Dimer, oxidation moves the major groove recognition alpha helices of the HypR dimer about 4 Angstroem towards each other
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
Palm, Gottfried; Chi, Bui Khanh; Waack, Paul; Gronau, Katrin; Becher, Dörte; Albrecht, Dirk; Hinrichs, Winfried; Read, Randy and Antelmann, Haike Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR Nucleic Acid Research 2012, in press.
