HypR

• 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

Categories containing this gene/protein

transcription factors and their control

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:

Expression and regulation

• Operon: yybR(hypR)(according to DBTBS)

• Sigma factor:

• 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

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.