AdhR

• 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
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

transcription factors and their control, resistance against oxidative and electrophile stress

The gene

Basic information

• Locus tag: BSU27000

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:

• Localization: cytoplasmic

Database entries

• Structure:

• UniProt: O06008

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: adhR PubMed

• 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

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)