Difference between revisions of "AdhR"

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Revision as of 14:02, 16 May 2013

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

Gene name adhR
Synonyms yraB
Essential no
Product MerR/NmlR-family transcriptional activator
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
























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:
  • Protein family:MerR/NmlR-family of regulators
  • 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)