TnrA

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  • Description: transcriptional pleiotropic regulator (MerR family) involved in global nitrogen regulation

Gene name tnrA
Synonyms scgR
Essential no
Product transcription activator/ repressor (MerR family)
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:
tnrA
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:
  • 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

  • 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

Your additional remarks

References

Reviews


The TnrA regulon

Control of TnrA activity by the trigger enzyme GlnA

Other original publications

Maria A Schumacher, Naga Babu Chinnam, Bonnie Cuthbert, Nam K Tonthat, Travis Whitfill
Structures of regulatory machinery reveal novel molecular mechanisms controlling B. subtilis nitrogen homeostasis.
Genes Dev: 2015, 29(4);451-64
[PubMed:25691471] [WorldCat.org] [DOI] (I p)

Yasutaro Fujita, Takenori Satomura, Shigeo Tojo, Kazutake Hirooka
CcpA-mediated catabolite activation of the Bacillus subtilis ilv-leu operon and its negation by either CodY- or TnrA-mediated negative regulation.
J Bacteriol: 2014, 196(21);3793-806
[PubMed:25157083] [WorldCat.org] [DOI] (I p)

K P Fedorova, I S Sharafutdinov, E Iu Turbina, M I Bogachev, O N Il'inskaia, A R Kaiumov
[The C-terminus of transcription factor TnrA from Bacillus subtilis controls DNA-binding domain activity but is not required for dimerization].
Mol Biol (Mosk): 2013, 47(2);331-7
[PubMed:23808168] [WorldCat.org] [DOI] (P p)

Ksenia Fedorova, Airat Kayumov, Kathrin Woyda, Olga Ilinskaja, Karl Forchhammer
Transcription factor TnrA inhibits the biosynthetic activity of glutamine synthetase in Bacillus subtilis.
FEBS Lett: 2013, 587(9);1293-8
[PubMed:23535029] [WorldCat.org] [DOI] (I p)

Airat Kayumov, Annette Heinrich, Kseniya Fedorova, Olga Ilinskaya, Karl Forchhammer
Interaction of the general transcription factor TnrA with the PII-like protein GlnK and glutamine synthetase in Bacillus subtilis.
FEBS J: 2011, 278(10);1779-89
[PubMed:21435182] [WorldCat.org] [DOI] (I p)

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)

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