Crh

• Description: "Catabolite repression 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
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	9,2 kDa, 4.70
Gene length, protein length	255 bp, 85 amino acids
Immediate neighbours	yvcN, yvcL
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

transcription factors and their control, phosphoproteins

The gene

Basic information

• Locus tag: BSU34740

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: HPr family (according to Swiss-Prot) PtsH, HPr family

• Paralogous protein(s): HPr

Extended information on the protein

• Kinetic information:

• Domains: HPr domain (1–85)

• Modification: phosphorylation on Ser46 by HprK PubMed

• Cofactor(s):

• Effectors of protein activity:

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

• Localization:

Database entries

• Structure: 2AK7 (dimeric Crh-Ser46-P), 1ZVV (CcpA-Crh-DNA complex), 2RLZ (dimer), 1MU4, NCBI, dimer NCBI, CcpA-Crh-DNA complex NCBI, dimeric phosphor-Crh NCBI
• UniProt: O06976

• KEGG entry: [2]

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 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Stülke lab
  • pGP734 (C-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP382), 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 Görke lab

• FLAG-tag construct: GP69 (spc, based on pGP1331), available in the Boris Görke and Stülke labs

• Antibody: available in Görke lab

Labs working on this gene/protein

Boris Görke, University of Göttingen, Germany Homepage

Anne Galinier, University of Marseille, France

Wolfgang Hillen, Erlangen University, Germany Homepage

Richard Brennan, Houston, Texas, USA Homepage

References

Frédérique Pompeo, Jennifer Luciano, Anne Galinier
Interaction of GapA with HPr and its homologue, Crh: Novel levels of regulation of a key step of glycolysis in Bacillus subtilis?
J Bacteriol: 2007, 189(3);1154-7
[PubMed:17142398] [WorldCat.org] [DOI] (P p)

Maria A Schumacher, Gerald Seidel, Wolfgang Hillen, Richard G Brennan
Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation.
J Biol Chem: 2006, 281(10);6793-800
[PubMed:16316990] [WorldCat.org] [DOI] (P p)

Boris Görke, Elodie Foulquier, Anne Galinier
YvcK of Bacillus subtilis is required for a normal cell shape and for growth on Krebs cycle intermediates and substrates of the pentose phosphate pathway.
Microbiology (Reading): 2005, 151(Pt 11);3777-3791
[PubMed:16272399] [WorldCat.org] [DOI] (P p)

Boris Görke, Laetitia Fraysse, Anne Galinier
Drastic differences in Crh and HPr synthesis levels reflect their different impacts on catabolite repression in Bacillus subtilis.
J Bacteriol: 2004, 186(10);2992-5
[PubMed:15126459] [WorldCat.org] [DOI] (P p)

Michel Juy, François Penin, Adrien Favier, Anne Galinier, Roland Montserret, Richard Haser, Josef Deutscher, Anja Böckmann
Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr.
J Mol Biol: 2003, 332(4);767-76
[PubMed:12972249] [WorldCat.org] [DOI] (P p)

Jean-Pierre Lavergne, Jean-Michel Jault, Anne Galinier
Insights into the functioning of Bacillus subtilis HPr kinase/phosphatase: affinity for its protein substrates and role of cations and phosphate.
Biochemistry: 2002, 41(20);6218-25
[PubMed:12009882] [WorldCat.org] [DOI] (P p)

I Martin-Verstraete, J Deutscher, A Galinier
Phosphorylation of HPr and Crh by HprK, early steps in the catabolite repression signalling pathway for the Bacillus subtilis levanase operon.
J Bacteriol: 1999, 181(9);2966-9
[PubMed:10217795] [WorldCat.org] [DOI] (P p)

A Galinier, J Deutscher, I Martin-Verstraete
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(2);307-14
[PubMed:9973552] [WorldCat.org] [DOI] (P p)

A Galinier, J Haiech, M C Kilhoffer, M Jaquinod, J Stülke, J Deutscher, I Martin-Verstraete
The Bacillus subtilis crh gene encodes a HPr-like protein involved in carbon catabolite repression.
Proc Natl Acad Sci U S A: 1997, 94(16);8439-44
[PubMed:9237995] [WorldCat.org] [DOI] (P p)