Difference between revisions of "GlnA"

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* '''Domains:''' glutamate binding flap (aa 300 ... 306: protects unstable intermediates from abberant hydrolysis)
 
* '''Domains:''' glutamate binding flap (aa 300 ... 306: protects unstable intermediates from abberant hydrolysis)
  
−
* '''Modification:''' phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed],  ''in vitro'' phosphorylated by [[PrkC]] on Thr-26, Thr-147, Ser-207, and Thr-286 {{PubMed|20389117}}
+
* '''Modification:'''  
 +
** phosphorylated on ser/ thr/ tyr [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed]
 +
** ''in vitro'' phosphorylated by [[PrkC]] on Thr-26, Thr-147, Ser-207, and Thr-286 {{PubMed|20389117}}
  
 
* '''Cofactor(s):''' Mg(2+)
 
* '''Cofactor(s):''' Mg(2+)
  
−
* '''Effectors of protein activity:''' feedback inhibition by glutamine, glutamine binds the entrance site for glutamate
+
* '''Effectors of protein activity:'''  
 +
** feedback inhibition by glutamine, glutamine binds the entrance site for glutamate
 +
** activity is inhibited upon interaction with [[TnrA]] {{PubMed|23535029}}
  
 
* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
Line 158: Line 162:
  
 
==Original publications==
 
==Original publications==
−
<pubmed>19233925, 20389117,8799114,18195355, 11719184, 12139611, 2573733, 8636055, 19233925, 16493705, 16885465, 6141156 2906311 20656908 16055443 18331450 16547045 8093698 21435182</pubmed>
+
<pubmed>19233925, 20389117,8799114,18195355, 11719184, 12139611, 2573733, 8636055, 19233925, 16493705, 16885465, 6141156 2906311 20656908 16055443 18331450 16547045 8093698 21435182 23535029</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:24, 29 March 2013

Gene name glnA
Synonyms
Essential no
Product trigger enzyme: glutamine synthetase
Function glutamine biosynthesis, control of TnrA and GlnR activity
Gene expression levels in SubtiExpress: glnA
Interactions involving this protein in SubtInteract: GlnA
Metabolic function and regulation of this protein in SubtiPathways:
Ammonium/ glutamate
MW, pI 50 kDa, 4.874
Gene length, protein length 1332 bp, 444 aa
Immediate neighbours glnR, ynxB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GlnA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GlnA expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, glutamate metabolism, transcription factors and their control, trigger enzyme, phosphoproteins

This gene is a member of the following regulons

GlnR regulon, TnrA regulon

The gene

Basic information

  • Locus tag: BSU17460

Phenotypes of a mutant

auxotrophic for glutamine

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine (according to Swiss-Prot)
  • Protein family: glutamine synthetase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: K(M) for: Glu: 27 mM, ATP: 2.4 mM, ammonium: 0.18 mM; v(max): 3.7 µmol/min/mg
  • Domains: glutamate binding flap (aa 300 ... 306: protects unstable intermediates from abberant hydrolysis)
  • Modification:
    • phosphorylated on ser/ thr/ tyr PubMed
    • in vitro phosphorylated by PrkC on Thr-26, Thr-147, Ser-207, and Thr-286 PubMed
  • Cofactor(s): Mg(2+)
  • Effectors of protein activity:
    • feedback inhibition by glutamine, glutamine binds the entrance site for glutamate
    • activity is inhibited upon interaction with TnrA PubMed

Database entries

  • KEGG entry: [3]

Additional information

GlnA is a homooligomer of 12 subunits

Expression and regulation

  • Regulation:
    • expressed in the absence of glutamine (GlnR) PubMed
    • repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
  • Additional information:

Biological materials

  • Mutant: GP247 (cat), available in Stülke lab
  • Expression vector:
    • expression/ purification from E. coli, with N-terminal Strep-tag (in pGP172): pGP174, available in Stülke lab
  • 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)


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)

Lewis V Wray, Susan H Fisher
Functional roles of the conserved Glu304 loop of Bacillus subtilis glutamine synthetase.
J Bacteriol: 2010, 192(19);5018-25
[PubMed:20656908] [WorldCat.org] [DOI] (I p)

Nico Pietack, Dörte Becher, Sebastian R Schmidl, Milton H Saier, Michael Hecker, Fabian M Commichau, Jörg Stülke
In vitro phosphorylation of key metabolic enzymes from Bacillus subtilis: PrkC phosphorylates enzymes from different branches of basic metabolism.
J Mol Microbiol Biotechnol: 2010, 18(3);129-40
[PubMed:20389117] [WorldCat.org] [DOI] (I p)

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
Bacillus subtilis GlnR contains an autoinhibitory C-terminal domain required for the interaction with glutamine synthetase.
Mol Microbiol: 2008, 68(2);277-85
[PubMed:18331450] [WorldCat.org] [DOI] (I p)

Susan H Fisher, Lewis V Wray
Bacillus subtilis glutamine synthetase regulates its own synthesis by acting as a chaperone to stabilize GlnR-DNA complexes.
Proc Natl Acad Sci U S A: 2008, 105(3);1014-9
[PubMed:18195355] [WorldCat.org] [DOI] (I 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)

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)

Lewis V Wray, Susan H Fisher
A feedback-resistant mutant of Bacillus subtilis glutamine synthetase with pleiotropic defects in nitrogen-regulated gene expression.
J Biol Chem: 2005, 280(39);33298-304
[PubMed:16055443] [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)

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, C A Rostkowski, E M Kellner
Altered regulation of the glnRA operon in a Bacillus subtilis mutant that produces methionine sulfoximine-tolerant glutamine synthetase.
J Bacteriol: 1993, 175(3);892-7
[PubMed:8093698] [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)

M A Strauch, A I Aronson, S W Brown, H J Schreier, A L Sonenhein
Sequence of the Bacillus subtilis glutamine synthetase gene region.
Gene: 1988, 71(2);257-65
[PubMed:2906311] [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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