Difference between revisions of "HypR"
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|style="background:#ABCDEF;" align="center"| '''Product''' || MarR/DUF24-family transcription regulator HypR | |style="background:#ABCDEF;" align="center"| '''Product''' || MarR/DUF24-family transcription regulator HypR | ||
|- | |- | ||
− | |style="background:#ABCDEF;" align="center"|'''Function''' || positively controls nitroreductase gene hypO | + | |style="background:#ABCDEF;" align="center"|'''Function''' || positively controls nitroreductase gene yfkO (hypO) in response to disulfide stress (diamide, NaOCl) |
|- | |- | ||
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 14 kDa, 8.415 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 14 kDa, 8.415 | ||
Line 45: | Line 45: | ||
===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 130: | Line 130: | ||
=References= | =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 | Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR | ||
Nucleic Acid Research 2012, in press. | Nucleic Acid Research 2012, in press. | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:41, 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 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
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.