CggR

• Description: repressor of the glycolytic gapA operon
  
  

Gene name	cggR
Synonyms	yvbQ
Essential	no
Product	central glycolytic genes regulator
Function	transcriptional regulator
MW, pI	37,2 kDa,5.68
Gene length, protein length	1020 bp, 340 amino acids
Immediate neighbours	araE, gapA
Gene sequence (+200bp)	Protein sequence
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates: 3481786 - 3482805

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: transcription repression of the glycolytic gapA operon

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:
  • DNA binding domain (H-T-H motif) (37–56)

• Modification:

• Cofactor(s):

• Effectors of protein activity: fructose 1.6-bisphosphate PubMed and dihydroxyacetone phosphate, glucose-6-phosphate and fructose-6-phosphate PubMed act as inducer and result in release of CggR from the DNA

• Interactions:

• Localization:

Database entries

• Structure: complex with Fructose-6-Phosphate NCBI, effector binding domain NCBI

• Swiss prot entry: [3]

• KEGG entry: [4]

Expression and regulation

• Operon:
  • cggR-gapA-pgk-tpiA-pgm-eno
  • cggR-gapA

The primary mRNAs of the operon are highly unstable. The primary mRNA is subject to processing at the very end of the cggR open reading frame. This results in stable mature gapA and gapA-pgk-tpiA-pgm-eno mRNAs. The processing event requires the Rny protein.

• Sigma factor: SigA

• Regulation: expression activated by glucose (76.76) PubMed, CggR represses the operon in the absence of glycolytic sugars PubMed

• Regulatory mechanism: repression

• Database entries: DBTBS

• Additional information:

Biological materials

• Mutant: GP311 (in frame deletion), available in Stülke lab

• Expression vector: pGP705 (N-terminal His-tag, in pWH844), available in Stülke lab

• lacZ fusion: pGP504 (in pAC7), pGP509 (in pAC6), available in Stülke lab

• GFP fusion:

• Antibody: available in Stülke lab

Labs working on this gene/protein

Stephane Aymerich, Microbiology and Molecular Genetics, INRA Paris-Grignon, France

References

1. Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
2. Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. subm.
3. Doan, T., and S. Aymerich. 2003. Regulation of the central glycolytic pathways in Bacillus subtilis: binding of the repressor CggR to its single DNA target sequence is modulated by fructose-1,6-bisphosphate. Mol. Microbiol. 47: 1709-1721. PubMed
4. Doan et al. (2008) A phospho-sugar binding domain homologous to NagB enzymes regulates the activity of the central glycolytic genes repressor. Proteins 71:2038-2050. PubMed
5. Fillinger, S., Boschi-Muller, S., Azza, S., Dervyn, E., Branlant, G., and Aymerich, S. (2000) Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. J Biol Chem 275, 14031-14037. PubMed
6. Ludwig, H., Homuth, G., Schmalisch, M., Dyka, F. M., Hecker, M., and Stülke, J. (2001) Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon. Mol Microbiol 41, 409-422.PubMed
7. Ludwig, H., Rebhan, N., Blencke, H.-M., Merzbacher, M. & Stülke, J. (2002). Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation. Mol Microbiol 45, 543-553.PubMed
8. Meinken, C., Blencke, H. M., Ludwig, H., and Stülke, J. (2003) Expression of the glycolytic gapA operon in Bacillus subtilis: differential synthesis of proteins encoded by the operon. Microbiology 149, 751-761. PubMed
9. Rezacova et al. (2008) Crystal structures of the effector-binding domain of repressor Central glycolytic gene Regulator from Bacillus subtilis reveal ligand-induced structural changes upon binding of several glycolytic intermediates. Mol. Microbiol. 69:895-910. PubMed
10. Zorilla et al. (2007) Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR). Biochemistry 46:14996-15008. PubMed
11. Zorilla et al. (2007) Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA. Biophys. J. 92: 3215-3227. PubMed