TnrA

• Description: transcriptional pleiotropic regulator invoved in global nitrogen regulation
  
  

Gene name	tnrA
Synonyms	scgR
Essential	no
Product	transcription activator/ repressor
Function	regulation of nitrogen assimilation
Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis, Nucleotides (regulation), Ile, Leu, Val, Ammonium/ glutamate, Central C-metabolism, Cell wall, Coenzyme A, Phosphorelay, Alternative nitrogen sources
MW, pI	12 kDa, 10.235
Gene length, protein length	330 bp, 110 aa
Immediate neighbours	mgtE, ykzB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, regulators of core metabolism

This gene is a member of the following regulons

GlnR regulon, TnrA regulon

The gene

Basic information

• Locus tag: BSU13310

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity: feedback-inhibited GlnA prevents TnrA from DNA binding

• Interactions: TnrA-NrgB PubMed, TnrA-GlnA, this interaction results in loss of TnrA DNA-binding activity PubMed

• Localization:

Database entries

• Structure:

• UniProt: Q45666

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: tnrA (according to DBTBS)

• Sigma factor:

• Regulation:
  • expression is autocativated (TnrA) and repressed by GlnR PubMed
  • expressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed

• Regulatory mechanism:
  • TnrA: transcription activation PubMed

• Additional information:

Biological materials

• Mutant: GP252 (in frame deletion), available in the Stülke lab

• Expression vector:
  • for expression, purification in E. coli with N-terminal His-tag, in pWH844: pGP171 available in Stülke lab
  • pGP229 (N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380), available in Stülke lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody: available in the Karl Forchhammer lab

Labs working on this gene/protein

Susan Fisher, Boston, USA homepage

References

Reviews

Fabian M Commichau, Jörg Stülke
Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression.
Mol Microbiol: 2008, 67(4);692-702
[PubMed:18086213] [WorldCat.org] [DOI] (P p)

S H Fisher
Regulation of nitrogen metabolism in Bacillus subtilis: vive la différence!
Mol Microbiol: 1999, 32(2);223-32
[PubMed:10231480] [WorldCat.org] [DOI] (P p)

The TnrA regulon

Ken-ichi Yoshida, Hirotake Yamaguchi, Masaki Kinehara, Yo-hei Ohki, Yoshiko Nakaura, Yasutaro Fujita
Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box.
Mol Microbiol: 2003, 49(1);157-65
[PubMed:12823818] [WorldCat.org] [DOI] (P p)

Control of TnrA activity by the trigger enzyme GlnA

Susan H Fisher, Lewis V Wray
Novel trans-Acting Bacillus subtilis glnA mutations that derepress glnRA expression.
J Bacteriol: 2009, 191(8);2485-92
[PubMed:19233925] [WorldCat.org] [DOI] (I p)

Lewis V Wray, Susan H Fisher
Functional analysis of the carboxy-terminal region of Bacillus subtilis TnrA, a MerR family protein.
J Bacteriol: 2007, 189(1);20-7
[PubMed:17085574] [WorldCat.org] [DOI] (P p)

Susan H Fisher, Lewis V Wray
Feedback-resistant mutations in Bacillus subtilis glutamine synthetase are clustered in the active site.
J Bacteriol: 2006, 188(16);5966-74
[PubMed:16885465] [WorldCat.org] [DOI] (P p)

Susan H Fisher, Jaclyn L Brandenburg, Lewis V Wray
Mutations in Bacillus subtilis glutamine synthetase that block its interaction with transcription factor TnrA.
Mol Microbiol: 2002, 45(3);627-35
[PubMed:12139611] [WorldCat.org] [DOI] (P p)

L V Wray, J M Zalieckas, S H Fisher
Bacillus subtilis glutamine synthetase controls gene expression through a protein-protein interaction with transcription factor TnrA.
Cell: 2001, 107(4);427-35
[PubMed:11719184] [WorldCat.org] [DOI] (P p)