AdhR

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  • Description: transcriptional activator (MerR family) of adhA-yraA, responsive to formaldehyde and methylglyoxal

Gene name adhR
Synonyms yraB
Essential no
Product transcriptional activator (MerR family)
Function regulation of the protective response to formaldehyde and methylglyoxal
Gene expression levels in SubtiExpress: adhR
MW, pI 16 kDa, 9.637
Gene length, protein length 420 bp, 140 aa
Immediate neighbours yraD, yrzP
Sequences Protein DNA DNA_with_flanks
Genetic context
YraB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AdhR expression.png

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 gene

Basic information

  • Locus tag: BSU27000

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: activity probably redox-controlled via thiol-(S)-alkylation at Cys-52 by aldehydes PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • 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

Alastair G McEwan, Karrera Y Djoko, Nathan H Chen, Rafael L M Couñago, Stephen P Kidd, Adam J Potter, Michael P Jennings
Novel bacterial MerR-like regulators their role in the response to carbonyl and nitrosative stress.
Adv. Microb. Physiol.: 2011, 58;1-22
[PubMed:21722790] [WorldCat.org] [DOI] (I p)

Antelmann H, Helmann JD.
Thiol-based redox switches and gene regulation.
Antioxid Redox Signal. 2011,14:1049-63.
PubMed

Original articles

Thi Thu Huyen Nguyen, Warawan Eiamphungporn, Ulrike Mäder, Manuel Liebeke, Michael Lalk, Michael Hecker, John D Helmann, Haike Antelmann
Genome-wide responses to carbonyl electrophiles in Bacillus subtilis: control of the thiol-dependent formaldehyde dehydrogenase AdhA and cysteine proteinase YraA by the MerR-family regulator YraB (AdhR).
Mol. Microbiol.: 2009, 71(4);876-94
[PubMed:19170879] [WorldCat.org] [DOI] (I p)

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