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}} | ||
Line 157: | Line 157: | ||
<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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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
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):
- Localization: membrane-associated via NrgA-NrgB under conditions of poor nitrogen supply PubMed
Database entries
- Structure:
- UniProt: Q45666
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Operon: tnrA (according to DBTBS)
- Regulation:
- Additional information:
Biological materials
- Mutant: GP252 (in frame deletion), available in the Stülke lab
- Expression vector:
- 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
Your additional remarks
References
Reviews
The TnrA regulon
Control of TnrA activity by the trigger enzyme GlnA
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)