GltC

• 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 This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates: 2013989 - 2014888

Phenotypes of a mutant

gltC mutants are auxotrophic for glutamate.

Database entries

• DBTBS entry: [1]

• SubtiList entry:[2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: transcription activation of the gltA-gltB 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 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:

• Swiss prot entry: P39812

• KEGG entry: [3]

Expression and regulation

• Operon: gltC

• Sigma factor: SigA

• Regulation: autoregulation by GltC

• Regulatory mechanism: autorepression

• Database entries: DBTBS

• 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

References

1. 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. PubMed
2. Belitsky, B. R., and Sonenshein, A. L. (1995) Mutations in GltC that increase Bacillus subtilis gltA expression. J Bacteriol 177: 5696-5700.PubMed
3. 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
4. Bohannon, D. E., and Sonenshein, A. L. (1989) Positive regulation of glutamate biosynthesis in Bacillus subtilis. J Bacteriol 171: 4718-4727.PubMed
5. 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
6. 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
7. 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
8. 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
9. 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. PubMed
10. Schell, M. A. (1993). Molecular biology of the LysR family of transcriptional regulators. Annu Rev Microbiol 47, 597-626. PubMed