Difference between revisions of "GltC"

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<pubmed>7559360 15150225 2548995 17183217 17608797 17134717 14523131, </pubmed>
 
<pubmed>7559360 15150225 2548995 17183217 17608797 17134717 14523131, </pubmed>
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# Yoshida K, et al. (2003) Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box. ''Mol Microbiol'' '''49(1):''' 157-65. [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+12823818 PubMed]
 
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# Belitsky, B. R., and Sonenshein, A. L. (1995) Mutations in GltC that increase ''Bacillus subtilis gltA'' expression. J Bacteriol 177: 5696-5700.[http://www.ncbi.nlm.nih.gov/sites/entrez/7559360 PubMed]
 
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# 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.[http://www.ncbi.nlm.nih.gov/sites/entrez/15150225 PubMed]
 
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# Bohannon, D. E., and Sonenshein, A. L. (1989) Positive regulation of glutamate biosynthesis in ''Bacillus subtilis''. J Bacteriol 171: 4718-4727.[http://www.ncbi.nlm.nih.gov/sites/entrez/2548995 PubMed]
 
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# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/17183217 PubMed]
 
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# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/17608797 PubMed] 
 
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# 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. [http://www.ncbi.nlm.nih.gov/sites/entrez/17134717 PubMed]
 
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# 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.[http://www.ncbi.nlm.nih.gov/sites/entrez/14523131 PubMed]
 
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# Herzberg, C., Flórez Weidinger, L. A., Dörrbecker, B., Hübner, S., Stülke, J. & Commichau, F. M. (2007) SPINE: A method for the rapid detection and analysis of protein-protein interactions in vivo. Proteomics 7: 4032-4035. [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17994626 PubMed]
 
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# Schell, M. A. (1993). Molecular biology of the LysR family of transcriptional regulators. Annu Rev Microbiol 47, 597-626. [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+8257110 PubMed]
 

Revision as of 17:16, 15 June 2009

  • Description: Transcriptional activator of the gltAB 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)
MW, pI 33.9 kDa, 5.62
Gene length, protein length 900 bp, 300 amino acids
Immediate neighbours gltA, proJ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GltC context.gif
This image was kindly provided by SubtiList






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

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: transcription activation of the gltA-gltB operon PubMed
  • Protein family: glutamate synthase family (according to Swiss-Prot) 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 stimulates transcription activation, glutamate inhibits transcription activation PubMed
  • Interactions:
    • 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
  • Localization:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: autoregulation by GltC
  • Regulatory mechanism: autorepression
  • Additional information:

Biological materials

  • Mutant: GP344 (erm), GP738 (spc) (available in Stülke lab)
  • Expression vector: pGP903 (in pWH844, N-terminal His-tag), pGP951 (C-terminal Strep-tag) (available in Stülke lab)
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody: available in Stülke lab

Labs working on this gene/protein

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

Jörg Stülke, University of Göttingen, Germany Homepage

Your additional remarks

References

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