Difference between revisions of "HypR"

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  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 Acids Res. 2012, Jan 11. [Epub ahead of print]
 
  Nucleic Acids Res. 2012, Jan 11. [Epub ahead of print]
{{PubMed|22238377}}
+
{{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
YybR context.gif
This image was kindly provided by SubtiList



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:
  • 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:
    • 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:
    • reduced HypRC14S dimer [3] PubMed
    • oxidized HypR C14-C49' intersubunit disulfide-linked dimer [4] PubMed
  • 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

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