Difference between revisions of "HypR"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU40540&redirect=T BSU40540]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yybR.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/yybR.html]
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU40540&redirect=T BSU40540]
  
 
* '''Structure:'''  
 
* '''Structure:'''  

Revision as of 16:17, 2 April 2014

  • 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)
Gene expression levels in SubtiExpress: hypR
MW, pI 14 kDa, 8.415
Gene length, protein length 375 bp, 125 aa
Immediate neighbours cotF, ppaC
Sequences Protein DNA DNA_with_flanks
Genetic context
YybR context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
HypR expression.png
























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

HypR regulon

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:

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
    • Cys14 and Cys49' are about 8-9 Angström 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
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
    • 4A5N (reduced HypRC14S dimer) PubMed
    • 4A5M (oxidized HypR C14-C49' intersubunit disulfide-linked dimer ) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
    • activated by disulfide stress conditions (diamide, NaOCl) in vivo and in vitro (autoregulation) PubMed
  • Regulatory mechanism:
    • HypR: transcription activation (autoregulation)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

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]
PubMed