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
Sequences	Protein DNA DNA_with_flanks
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)