TnrA

From SubtiWiki
Revision as of 10:01, 14 May 2013 by 134.76.70.252 (talk)
Jump to: navigation, search
  • 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
Gene expression levels in SubtiExpress: tnrA
Interactions involving this protein in SubtInteract: TnrA
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
Sequences Protein DNA DNA_with_flanks
Genetic context
TnrA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TnrA expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, glutamate metabolism, transcription factors and their control, regulators of core metabolism

This gene is a member of the following regulons

GlnR regulon, TnrA regulon

The TnrA regulon

The gene

Basic information

  • Locus tag: BSU13310

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

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

Extended information on the protein

  • Kinetic information:
    • K(D) value for the binding site in the tnrA promoter region: 55 nM PubMed
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: feedback-inhibited GlnA prevents TnrA from DNA binding

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon: tnrA (according to DBTBS)
  • 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:
  • 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:

Labs working on this gene/protein

Susan Fisher, Boston, USA homepage

Your additional remarks

References

Reviews

Katrin Gunka, Fabian M Commichau
Control of glutamate homeostasis in Bacillus subtilis: a complex interplay between ammonium assimilation, glutamate biosynthesis and degradation.
Mol Microbiol: 2012, 85(2);213-24
[PubMed:22625175] [WorldCat.org] [DOI] (I p)

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)

Other original publications