Difference between revisions of "GltC"

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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
 
** active as dimer
 
** active as dimer
** GltC-[[RocG]], This interaction takes place in the presence of glutamate. It prevents the transcription activation of the ''[[gltA]]-[[gltB]]'' operon. Note that [[RocG]] expression is strongly regulated by carbon and nitrogen sources, respectively. [http://www.ncbi.nlm.nih.gov/sites/entrez/17608797 PubMed]
+
** [[GltC]]-[[RocG]], This interaction takes place in the presence of glutamate. It prevents the transcription activation of the ''[[gltA]]-[[gltB]]'' operon. Note that [[RocG]] expression is strongly regulated by carbon and nitrogen sources, respectively {{PubMed|17608797}}
 +
** [[GltC]]-[[GudB]] {{PubMed|25711804}}
  
 
* '''[[Localization]]:'''
 
* '''[[Localization]]:'''
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=Biological materials =
 
=Biological materials =
  
* '''Mutant:''' GP344 (erm), GP738 (spc) (available in [[Stülke]] lab)
+
* '''Mutant:''' GP344 (erm), GP738 (spc) (available in [[Jörg Stülke]]'s lab)
  
 
* '''Expression vector:'''  
 
* '''Expression vector:'''  
** for expression, purification in ''E. coli'' with N-terminal His-tag, in [[pWH844]]: pGP903,  available in [[Stülke]] lab
+
** for expression, purification in ''E. coli'' with N-terminal His-tag, in [[pWH844]]: pGP903,  available in [[Jörg Stülke]]'s lab
** for expression, purification in ''E. coli'' with C-terminal Strep-tag, in pET3C: pGP951,  available in [[Stülke]] lab
+
** for expression, purification in ''E. coli'' with C-terminal Strep-tag, in pET3C: pGP951,  available in [[Jörg Stülke]]'s lab
 
 
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''
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* '''GFP fusion:'''
 
* '''GFP fusion:'''
  
* '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab
+
* '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Jörg Stülke]]'s lab
  
* '''Antibody:''' available in Stülke lab
+
* '''Antibody:''' available in [[Jörg Stülke]]'s lab
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
Line 161: Line 162:
  
 
==Original Publications==
 
==Original Publications==
<pubmed>7559360 15150225 2548995 17183217 17608797 17134717 14523131, 20630473</pubmed>
+
<pubmed>7559360 15150225 2548995 17183217 17608797 17134717 14523131, 20630473 25711804</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 13:00, 3 March 2015

  • Description: Transcriptional activator of the gltA-gltB operon. Activates expression of the operon in the absence of arginine.

Gene name gltC
Synonyms
Essential No
Product transcriptional regulator (LysR family)
Function positive regulation
of the glutamate synthase operon (gltAB)
Gene expression levels in SubtiExpress: gltC
Interactions involving this protein in SubtInteract: GltC
Metabolic function and regulation of this protein in SubtiPathways:
gltC
MW, pI 33.9 kDa, 5.62
Gene length, protein length 900 bp, 300 amino acids
Immediate neighbours gltA, proJ
Sequences Protein DNA DNA_with_flanks
Genetic context
GltC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
GltC expression.png















Categories containing this gene/protein

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

This gene is a member of the following regulons

The GltC regulon:

The gene

Basic information

  • Locus tag: BSU18460

Phenotypes of a mutant

gltC mutants are auxotrophic for glutamate.

Database entries

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

Additional information

Expression

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: transcription activation of the gltA-gltB operon PubMed
  • Paralogous protein(s): none, but there are 19 members of the LysR family in B. subtilis

Extended information on the protein

  • Kinetic information:
  • Domains: DNA-binding helix-turn-helix motif: AA 18 ... 37
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: 2-oxoglutarate stimulates transcription activation, glutamate inhibits transcription activation PubMed
  • Interactions:
    • active as dimer
    • GltC-RocG, This interaction takes place in the presence of glutamate. It prevents the transcription activation of the gltA-gltB operon. Note that RocG expression is strongly regulated by carbon and nitrogen sources, respectively PubMed
    • GltC-GudB PubMed

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: autoregulation by GltC PubMed
  • Regulatory mechanism: autorepression PubMed
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 43 PubMed

Biological materials

  • Mutant: GP344 (erm), GP738 (spc) (available in Jörg Stülke's lab)
  • Expression vector:
    • for expression, purification in E. coli with N-terminal His-tag, in pWH844: pGP903, available in Jörg Stülke's lab
    • for expression, purification in E. coli with C-terminal Strep-tag, in pET3C: pGP951, available in Jörg Stülke's lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab

Labs working on this gene/protein

Linc Sonenshein, Tufts University, Boston, MA, USA Homepage

Jörg Stülke, University of Göttingen, Germany Homepage

Fabian Commichau University of Göttingen, Germany Homepage

Your additional remarks

References

Reviews


Original Publications

Lorena Stannek, Martin J Thiele, Till Ischebeck, Katrin Gunka, Elke Hammer, Uwe Völker, Fabian M Commichau
Evidence for synergistic control of glutamate biosynthesis by glutamate dehydrogenases and glutamate in Bacillus subtilis.
Environ Microbiol: 2015, 17(9);3379-90
[PubMed:25711804] [WorldCat.org] [DOI] (I p)

Katrin Gunka, Joseph A Newman, Fabian M Commichau, Christina Herzberg, Cecilia Rodrigues, Lorraine Hewitt, Richard J Lewis, Jörg Stülke
Functional dissection of a trigger enzyme: mutations of the bacillus subtilis glutamate dehydrogenase RocG that affect differentially its catalytic activity and regulatory properties.
J Mol Biol: 2010, 400(4);815-27
[PubMed:20630473] [WorldCat.org] [DOI] (I p)

Fabian M Commichau, Christina Herzberg, Philipp Tripal, Oliver Valerius, Jörg Stülke
A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: the glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC.
Mol Microbiol: 2007, 65(3);642-54
[PubMed:17608797] [WorldCat.org] [DOI] (P p)

Fabian M Commichau, Ingrid Wacker, Jan Schleider, Hans-Matti Blencke, Irene Reif, Philipp Tripal, Jörg Stülke
Characterization of Bacillus subtilis mutants with carbon source-independent glutamate biosynthesis.
J Mol Microbiol Biotechnol: 2007, 12(1-2);106-13
[PubMed:17183217] [WorldCat.org] [DOI] (P p)

Silvia Picossi, Boris R Belitsky, Abraham L Sonenshein
Molecular mechanism of the regulation of Bacillus subtilis gltAB expression by GltC.
J Mol Biol: 2007, 365(5);1298-313
[PubMed:17134717] [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)

Ingrid Wacker, Holger Ludwig, Irene Reif, Hans-Matti Blencke, Christian Detsch, Jörg Stülke
The regulatory link between carbon and nitrogen metabolism in Bacillus subtilis: regulation of the gltAB operon by the catabolite control protein CcpA.
Microbiology (Reading): 2003, 149(Pt 10);3001-3009
[PubMed:14523131] [WorldCat.org] [DOI] (P p)

B R Belitsky, A L Sonenshein
Mutations in GltC that increase Bacillus subtilis gltA expression.
J Bacteriol: 1995, 177(19);5696-700
[PubMed:7559360] [WorldCat.org] [DOI] (P p)

D E Bohannon, A L Sonenshein
Positive regulation of glutamate biosynthesis in Bacillus subtilis.
J Bacteriol: 1989, 171(9);4718-27
[PubMed:2548995] [WorldCat.org] [DOI] (P p)