Difference between revisions of "HypR"
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{{SubtiWiki category|[[transcription factors and their control]]}}, | {{SubtiWiki category|[[transcription factors and their control]]}}, | ||
{{SubtiWiki category|[[resistance against oxidative and electrophile stress]]}} | {{SubtiWiki category|[[resistance against oxidative and electrophile stress]]}} | ||
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= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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==Reviews== | ==Reviews== | ||
− | + | ||
− | + | Antelmann H, Helmann JD. | |
+ | Thiol-based redox switches and gene regulation. | ||
+ | Antioxid Redox Signal. 2011,14:1049-63. | ||
+ | {{PubMed|20626317}} | ||
==Original articles== | ==Original articles== | ||
− | + | ||
− | + | Palm GJ, Khanh Chi B, Waack P, Gronau K, Becher D, Albrecht D, Hinrichs W, Read RJ, Antelmann H. | |
− | + | Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR. | |
+ | Nucleic Acids Res. 2012, Jan 11. [Epub ahead of print] | ||
+ | {{PubMed|22238377}} | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 19:49, 16 January 2012
- Description: MarR/DUF24-family transcription regulator, positively controls the nitroreductase gene hypO in response to disulfide stress
Gene name | hypR |
Synonyms | yybR |
Essential | no |
Product | MarR/DUF24-family transcription regulator HypR |
Function | control of the nitroreductase gene 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
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Contents
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
The HypR regulon:
The gene
Basic information
- Locus tag: BSU40540
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
hypR is autoregulated by disulfide stress
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: MarR/DUF24-family regulator
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:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cytoplasmic
Database entries
- Structure:
- UniProt: P37486
- KEGG entry: [5]
- E.C. number:
Additional information
Expression and regulation
- Operon: 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 in vivo PubMed
- Additional information:
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
Reviews
Antelmann H, Helmann JD. Thiol-based redox switches and gene regulation. Antioxid Redox Signal. 2011,14:1049-63. PubMed
Original articles
Palm GJ, Khanh Chi B, Waack P, Gronau K, Becher D, Albrecht D, Hinrichs W, Read RJ, Antelmann H. Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR. Nucleic Acids Res. 2012, Jan 11. [Epub ahead of print]