Difference between revisions of "HypR"

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* '''Description:''' MarR/DUF24-family transcription regulator <br/><br/>
+
* '''Description:''' MarR/DUF24-family transcription regulator, positively controls the nitroreductase gene ''yfkO''(hypO) in response to disulfide stress <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
|''yybR''
+
|''yybR''(hypR)
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
+
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''hypR''
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Product''' || MarR/DUF24-family transcription regulator   
+
|style="background:#ABCDEF;" align="center"| '''Product''' || MarR/DUF24-family transcription regulator HypR  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || unknown
+
|style="background:#ABCDEF;" align="center"|'''Function''' || positively controls nitroreductase gene hypO (yfkO) 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   
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===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 ===
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=== Additional information===
 
=== Additional information===
  
 
+
* '''hypR autoregulated by disulfide stress
  
  
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* '''Catalyzed reaction/ biological activity:'''  
 
* '''Catalyzed reaction/ biological activity:'''  
  
* '''Protein family:'''
+
* '''Protein family:'''MarR/DUF24-family regulator
  
* '''Paralogous protein(s):'''
+
* '''Paralogous protein(s):'''YdeP,YkvN
  
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
  
* '''Kinetic information:'''
+
* '''Kinetic information:'''Cys14 redox sensing Cys, has lower pKa of 6.36
  
* '''Domains:'''  
+
* '''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:'''
+
* '''Modification:'''oxidized to Cys14-Cys49' intersubunit disulfides by disulfide stress
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
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* '''Interactions:'''
 
* '''Interactions:'''
  
* '''Localization:'''
+
* '''Localization:'''cytoplasmic
  
 
=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
+
* '''Structure:'''tba
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37486 P37486]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37486 P37486]
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=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:''' ''yybR'' (according to [http://dbtbs.hgc.jp/COG/prom/yybR.html DBTBS])
+
* '''Operon:''' ''yybR''(hypR)(according to [http://dbtbs.hgc.jp/COG/prom/yybR.html DBTBS])
  
 
* '''[[Sigma factor]]:'''  
 
* '''[[Sigma factor]]:'''  
  
* '''Regulation:'''  
+
* '''Regulation:'''activated by disulfide stress conditions (diamide, NaOCl) in vivo and in vitro
  
* '''Regulatory mechanism:'''  
+
* '''Regulatory mechanism:'''redox-controlled by Cys14-Cys49' intersubunit disulfide formation by diamide and NaOCl in vitro and vivo
  
* '''Additional information:'''
+
* '''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 =
 
=Biological materials =
Line 127: Line 129:
  
 
=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
 +
Nucleic Acid Research 2012, in press.
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:32, 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 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
YybR context.gif
This image was kindly provided by SubtiList



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
  • 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.