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
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
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, transcription factors and their control, 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]

Additional information

Expression

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: membrane-associated via NrgA-NrgB under conditions of poor nitrogen supply PubMed

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)

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

Additional publications: PubMed

Airat Kayumov, Annette Heinrich, Margarita Sharipova, Olga Iljinskaya, Karl Forchhammer
Inactivation of the general transcription factor TnrA in Bacillus subtilis by proteolysis.
Microbiology (Reading): 2008, 154(Pt 8);2348-2355
[PubMed:18667567] [WorldCat.org] [DOI] (P p)

Annette Heinrich, Kathrin Woyda, Katja Brauburger, Gregor Meiss, Christian Detsch, Jörg Stülke, Karl Forchhammer
Interaction of the membrane-bound GlnK-AmtB complex with the master regulator of nitrogen metabolism TnrA in Bacillus subtilis.
J Biol Chem: 2006, 281(46);34909-17
[PubMed:17001076] [WorldCat.org] [DOI] (P p)

Jill M Zalieckas, Lewis V Wray, Susan H Fisher
Cross-regulation of the Bacillus subtilis glnRA and tnrA genes provides evidence for DNA binding site discrimination by GlnR and TnrA.
J Bacteriol: 2006, 188(7);2578-85
[PubMed:16547045] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Shigeo Tojo, Takenori Satomura, Kaori Morisaki, Ken-Ichi Yoshida, Kazutake Hirooka, Yasutaro Fujita
Negative transcriptional regulation of the ilv-leu operon for biosynthesis of branched-chain amino acids through the Bacillus subtilis global regulator TnrA.
J Bacteriol: 2004, 186(23);7971-9
[PubMed:15547269] [WorldCat.org] [DOI] (P p)

Boris R Belitsky, Abraham L Sonenshein
Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase.
J Bacteriol: 2004, 186(11);3399-407
[PubMed:15150225] [WorldCat.org] [DOI] (P p)

Emmanuel Guedon, Charles M Moore, Qiang Que, Tao Wang, Rick W Ye, John D Helmann
The global transcriptional response of Bacillus subtilis to manganese involves the MntR, Fur, TnrA and sigmaB regulons.
Mol Microbiol: 2003, 49(6);1477-91
[PubMed:12950915] [WorldCat.org] [DOI] (P p)

Jaclyn L Brandenburg, Lewis V Wray, Lars Beier, Hanne Jarmer, Hans H Saxild, Susan H Fisher
Roles of PucR, GlnR, and TnrA in regulating expression of the Bacillus subtilis ure P3 promoter.
J Bacteriol: 2002, 184(21);6060-4
[PubMed:12374841] [WorldCat.org] [DOI] (P p)

B R Belitsky, L V Wray, S H Fisher, D E Bohannon, A L Sonenshein
Role of TnrA in nitrogen source-dependent repression of Bacillus subtilis glutamate synthase gene expression.
J Bacteriol: 2000, 182(21);5939-47
[PubMed:11029411] [WorldCat.org] [DOI] (P p)

D Robichon, M Arnaud, R Gardan, Z Pragai, M O'Reilly, G Rapoport, M Débarbouillé
Expression of a new operon from Bacillus subtilis, ykzB-ykoL, under the control of the TnrA and PhoP-phoR global regulators.
J Bacteriol: 2000, 182(5);1226-31
[PubMed:10671441] [WorldCat.org] [DOI] (P p)

L V Wray, A E Ferson, S H Fisher
Expression of the Bacillus subtilis ureABC operon is controlled by multiple regulatory factors including CodY, GlnR, TnrA, and Spo0H.
J Bacteriol: 1997, 179(17);5494-501
[PubMed:9287005] [WorldCat.org] [DOI] (P p)

L V Wray, A E Ferson, K Rohrer, S H Fisher
TnrA, a transcription factor required for global nitrogen regulation in Bacillus subtilis.
Proc Natl Acad Sci U S A: 1996, 93(17);8841-5
[PubMed:8799114] [WorldCat.org] [DOI] (P p)

S W Brown, A L Sonenshein
Autogenous regulation of the Bacillus subtilis glnRA operon.
J Bacteriol: 1996, 178(8);2450-4
[PubMed:8636055] [WorldCat.org] [DOI] (P p)

H J Schreier, S W Brown, K D Hirschi, J F Nomellini, A L Sonenshein
Regulation of Bacillus subtilis glutamine synthetase gene expression by the product of the glnR gene.
J Mol Biol: 1989, 210(1);51-63
[PubMed:2573733] [WorldCat.org] [DOI] (P p)

S H Fisher, A L Sonenshein
Bacillus subtilis glutamine synthetase mutants pleiotropically altered in glucose catabolite repression.
J Bacteriol: 1984, 157(2);612-21
[PubMed:6141156] [WorldCat.org] [DOI] (P p)