Crh

• Description: "Catabolite rpression HPr-like protein", Cofactor of the CcpA transcription factor
  
  

Gene name	crh
Synonyms	yvcM
Essential	no
Product	catabolite repression HPr-like protein
Function	catabolite repression
MW, pI	9,2 kDa, 4.70
Gene length, protein length	255 bp, 85 amino acids
Immediate neighbours	yvcL, yvcN
Gene sequence (+200bp)	Protein sequence
Genetic context

The gene

Basic information

• Coordinates: 3568325 - 3568579

Database entries

• DBTBS entry:

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: PtsH,HPr family

• Paralogous protein(s): HPr

Extended information on the protein

• Kinetic information:

• Domains: HPr domain (1–85)

• Modification: phosphorylation at Ser46 by HPrK

• Cofactor(s):

• Effectors of protein activity:

• Interactions: Crh-GapA PubMed, Crh-CcpA PubMed, HprK-Crh PubMed

• Localization:

Database entries

• Structure: NCBI, dimer NCBI, CcpA-Crh-DNA complex NCBI, dimeric phosphor-Crh NCBI
• Swiss prot entry: [2]

• KEGG entry: [3]

Additional information

Crh does not possess the phosphorylation site used for PTS phosphotransfer (His-15 in PtsH), it can only be phosphorylated on Ser-46

Expression and regulation

• Operon: yvcI-yvcJ-yvcK-yvcL-crh-yvcN PubMed

• Sigma factor: SigA PubMed

• Regulation: very weak stimuation of expression by citrate and succinate PubMed

• Regulatory mechanism:

• Additional information: Crh is weakly expressed. This results in part from a poorly conserved ribosomal binding site of the mRNA. PubMed

Biological materials

• Mutant: GP860 (aphA3), QB7097 (spc), available in Stülke lab

• Expression vector: pGP641 (in pGP380, for SPINE, expression in B. subtilis), pGP734 (in pGP380, for SPINE, expression in B. subtilis), available in Stülke lab

• lacZ fusion: see yvcI

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab

• Antibody: available in Stülke lab (not very good)

Labs working on this gene/protein

Boris Görke, University of Göttingen, Germany Homepage

Anne Galinier, University of Marseille, France

References

1. Juy M, Penin F, Favier A (2003) Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr. J Mol Biol. 332(4):767-76. PubMed
2. Galinier A, Deutscher J, Martin-Verstraete I: Phosphorylation of either Crh or HPr mediates binding of CcpA to the Bacillus subtilis xyn cre and catabolite repression of the xyn operon. J Mol Biol 1999, 286:307-314. PubMed
3. Galinier, A., Haiech, J., Kilhoffer, M.-C., Jaquinod, M., Stülke, J., Deutscher, J., & Martin-Verstraete, I. (1997) The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression. Proc. Natl. Acad. Sci. USA 94: 8439-8444. PubMed
4. Görke, B., Fraysse, L. & Galinier, A. Drastic differences in Crh and HPr synthesis levels reflect their different impacts on catabolite repression in Bacillus subtilis. J. Bacteriol. 186, 2992-2995 (2004). PubMed
5. Martin-Verstraete, I., Deutscher, J., and Galinier, A. (1999) Phosphorylation of HPr and Crh by HprK, early steps in the catabolite repression signalling pathway for the Bacillus subtilis levanase operon. J Bacteriol 181: 2966-2969. PubMed
6. Pompeo et al. (2007) Interaction of GapA with HPr and its homologue, Crh: Novel levels of regulation of a key step of glycolysis in Bacillus subtilis? J Bacteriol 189, 1154-1157.PubMed
7. Schumacher, M. A., Seidel, G., Hillen, W. & Brennan, R. G. Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation. J. Biol. Chem. 281, 6793-6800 (2006). PubMed