Difference between revisions of "Crh"

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(Biological materials)
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** pGP1200 ''crh''(Ser46Ala) (spc, based on [[pGP1331]]), available in the [[Stülke]] lab
 
** pGP1200 ''crh''(Ser46Ala) (spc, based on [[pGP1331]]), available in the [[Stülke]] lab
  
* '''Antibody:''' available in [[Boris Görke| Görke]] lab
 
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=

Revision as of 10:15, 10 November 2011

  • Description: "Catabolite repression HPr-like protein", control of flux through the harmful methylglyoxal pathway, minor cofactor of the CcpA transcription factor

Gene name crh
Synonyms yvcM
Essential no
Product catabolite repression HPr-like protein
Function control of carbon flux
Interactions involving this protein in SubtInteract: Crh
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
Crh context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

transcription factors and their control, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU34740

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: 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:

Database entries


  • 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

  • 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: crh, crh(Ser46Asp), crh(Ser46Ala) B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), 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

Your additional remarks

References

Jens J Landmann, Ricarda A Busse, Jan-Hendrik Latz, Kalpana D Singh, Jörg Stülke, Boris Görke
Crh, the paralogue of the phosphocarrier protein HPr, controls the methylglyoxal bypass of glycolysis in Bacillus subtilis.
Mol. Microbiol.: 2011, 82(3);770-87
[PubMed:21992469] [WorldCat.org] [DOI] (I p)

Carole Gardiennet, Antoine Loquet, Manuel Etzkorn, Henrike Heise, Marc Baldus, Anja Böckmann
Structural constraints for the Crh protein from solid-state NMR experiments.
J. Biomol. NMR: 2008, 40(4);239-50
[PubMed:18320329] [WorldCat.org] [DOI] (P p)

Antoine Loquet, Benjamin Bardiaux, Carole Gardiennet, Christophe Blanchet, Marc Baldus, Michael Nilges, Thérèse Malliavin, Anja Böckmann
3D structure determination of the Crh protein from highly ambiguous solid-state NMR restraints.
J. Am. Chem. Soc.: 2008, 130(11);3579-89
[PubMed:18284240] [WorldCat.org] [DOI] (I p)

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)

Vincent Chaptal, Laurent Larivière, Virginie Gueguen-Chaignon, Anne Galinier, Sylvie Nessler, Solange Moréra
X-ray structure of a domain-swapped dimer of Ser46-phosphorylated Crh from Bacillus subtilis.
Proteins: 2006, 63(1);249-51
[PubMed:16411239] [WorldCat.org] [DOI] (I 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, Engl.): 2005, 151(Pt 11);3777-91
[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)

Jessica B Warner, Juke S Lolkema
A Crh-specific function in carbon catabolite repression in Bacillus subtilis.
FEMS Microbiol. Lett.: 2003, 220(2);277-80
[PubMed:12670692] [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)

Adrien Favier, Bernhard Brutscher, Martin Blackledge, Anne Galinier, Josef Deutscher, François Penin, Dominique Marion
Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr.
J. Mol. Biol.: 2002, 317(1);131-44
[PubMed:11916384] [WorldCat.org] [DOI] (P p)

E Darbon, A Galinier, D Le Coq, J Deutscher
Phosphotransfer functions mutated Bacillus subtilis HPr-like protein Crh carrying a histidine in the active site.
J. Mol. Microbiol. Biotechnol.: 2001, 3(3);439-44
[PubMed:11361076] [WorldCat.org] (P p)

F Penin, A Favier, R Montserret, B Brutscher, J Deutscher, D Marion, D Galinier
Evidence for a dimerisation state of the Bacillus subtilis catabolite repression HPr-like protein, Crh.
J. Mol. Microbiol. Biotechnol.: 2001, 3(3);429-32
[PubMed:11361074] [WorldCat.org] (P p)

I Martin-Verstraete, A Galinier, E Darbon, Y Quentin, M C Kilhoffer, V Charrier, J Haiech, G Rapoport, J Deutscher
The Q15H mutation enables Crh, a Bacillus subtilis HPr-like protein, to carry out some regulatory HPr functions, but does not make it an effective phosphocarrier for sugar transport.
Microbiology (Reading, Engl.): 1999, 145 ( Pt 11);3195-204
[PubMed:10589728] [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] (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)