Difference between revisions of "GltC"

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(Extended information on the protein)
(Labs working on this gene/protein)
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=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
  
Linc Sonenshein, Tufts University, Boston, MA, USA [http://www.tufts.edu/sackler/microbiology/faculty/sonenshein/index.html]
+
[[Linc Sonenshein|Linc Sonenshein]], Tufts University, Boston, MA, USA [http://www.tufts.edu/sackler/microbiology/faculty/sonenshein/index.html]
  
 
[[Stülke|Jörg Stülke]], University of Göttingen, Germany
 
[[Stülke|Jörg Stülke]], University of Göttingen, Germany

Revision as of 15:00, 15 December 2008

  • Synonyms:
  • Description: Transcriptional activator of the gltAB operon. Activates expression of the operon in the absence of arginine.


The gene

Basic information

  • Coordinates:
  • Gene length:

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: transcription activation of the gltAB operon PubMed
  • Protein family: LysR-type transcription regulator 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 PubMed
  • Interactions:
    • GltC-RocG, This interaction takes place in the presence of glutamate. It prevents the transcription activation of the gltAB operon. Note that RocG expression is strongly regulated. PubMed
  • Localization:

Database entries

  • Structure:

Additional information

Expression and regulation

  • Operon: gltC
  • Sigma factor: SigA
  • Regulation: autoregulation by GltC
  • Regulatory mechanism: autorepression
  • Additional information:

Biological materials

  • Mutant: GP344 (erm), GP738 (spc) (available in Stülke lab)
  • Expression vector: pGP903 (N-terminal His-tag) (available in Stülke lab)
  • lacZ fusion:
  • GFP fusion:
  • Antibody: available in Stülke lab

Labs working on this gene/protein

Linc Sonenshein, Tufts University, Boston, MA, USA [3]

Jörg Stülke, University of Göttingen, Germany [4]

Your additional remarks

References

  1. Belitsky, B. R., and Sonenshein, A. L. (1995) Mutations in GltC that increase Bacillus subtilis gltA expression. J Bacteriol 177: 5696-5700.PubMed
  2. Belitsky, B. R., and Sonenshein, A. L. (2004) Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase. J Bacteriol 186: 3399-3407.PubMed
  3. Bohannon, D. E., and Sonenshein, A. L. (1989) Positive regulation of glutamate biosynthesis in Bacillus subtilis. J Bacteriol 171: 4718-4727.PubMed
  4. Commichau, F. M., Wacker, I., Schleider, J., Blencke, H.-M., Reif, I., Tripal, P., and Stülke, J. (2007) Characterization of Bacillus subtilis mutants with carbon source-independent glutamate biosynthesis. J Mol Microbiol Biotechnol 12: 106-113. PubMed
  5. Commichau, F. M., Herzberg, C., Tripal, P., Valerius, O., and Stülke, J. (2007) A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: The glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC. Mol Microbiol 65: 642-654. PubMed
  6. Picossi, S., Belitsky, B. R., and Sonenshein, A. L. (2007) Molecular mechanism of the regulation of Bacillus subtilis gltAB expression by GltC. J Mol Biol 365: 1298-1313. PubMed
  7. Wacker, I., Ludwig, H., Reif, I., Blencke, H. M., Detsch, C., and Stülke, J. (2003) The regulatory link between carbon and nitrogen metabolism in Bacillus subtilis: regulation of the gltAB operon by the catabolite control protein CcpA. Microbiology 149: 3001-3009.PubMed