Difference between revisions of "TnrA"

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* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
  
−
* '''Effectors of protein activity:''' feedback-inhibited [[GlnA]] prevents TnrA from DNA binding
+
* '''Effectors of protein activity:''' feedback-inhibited [[GlnA]] prevents [[TnrA]] from DNA binding
  
 
* '''[[SubtInteract|Interactions]]:'''  
 
* '''[[SubtInteract|Interactions]]:'''  
 
** [[TnrA]]-[[NrgB]]  [http://www.ncbi.nlm.nih.gov/sites/entrez/17001076 PubMed]
 
** [[TnrA]]-[[NrgB]]  [http://www.ncbi.nlm.nih.gov/sites/entrez/17001076 PubMed]
−
** [[TnrA]]-[[GlnA]], this interaction results in loss of [[TnrA]] DNA-binding activity {{PubMed|11719184}}
+
** [[TnrA]]-[[GlnA]], this interaction results in loss of [[TnrA]] DNA-binding activity as well as in inhibition of [[GlnA]] {{PubMed|23535029,11719184}}  
  
 
* '''[[Localization]]:''' membrane-associated via [[NrgA]]-[[NrgB]] under conditions of poor nitrogen supply {{PubMed|21435182}}
 
* '''[[Localization]]:''' membrane-associated via [[NrgA]]-[[NrgB]] under conditions of poor nitrogen supply {{PubMed|21435182}}
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<pubmed>11719184, 12139611, 17085574 19233925, 16885465, </pubmed>
 
<pubmed>11719184, 12139611, 17085574 19233925, 16885465, </pubmed>
 
==Other original publications==
 
==Other original publications==
−
<pubmed>12374841,15547269,9287005, 12950915,10671441,16547045,16547045 ,8799114, 15150225, 11029411,17001076,15547269, 2573733, 8636055, 16493705, 6141156 18667567 21435182</pubmed>
+
<pubmed>12374841,15547269,9287005, 12950915,10671441,16547045,16547045 ,8799114, 15150225, 11029411,17001076,15547269, 2573733, 8636055, 16493705, 6141156 18667567 21435182 23535029</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:27, 29 March 2013

  • 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
Get the DNA and protein sequences
(Barbe et al., 2009)
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

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

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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