Difference between revisions of "CggR"
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:08, 23 April 2010
- Description: repressor of the glycolytic gapA operon, DeoR family
Gene name | cggR |
Synonyms | yvbQ |
Essential | no |
Product | central glycolytic genes regulator |
Function | transcriptional regulator |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 37,2 kDa,5.68 |
Gene length, protein length | 1020 bp, 340 amino acids |
Immediate neighbours | gapA, araE |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU33950
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: transcription repression of the glycolytic gapA operon
- Protein family: sorC transcriptional regulatory family (according to Swiss-Prot)
- 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: 2OKG ( effector binding domain), 3BXH (in complex with fructose-6-phosphate), complex with Fructose-6-Phosphate NCBI, effector binding domain NCBI
- UniProt: O32253
- KEGG entry: [3]
Additional information
Expression and regulation
- Database entries: DBTBS
- Additional information:
Biological materials
- Mutant:
- GP311 (in frame deletion), available in Stülke lab
- SM-NB7 (cggR-spc), available in Anne Galinier's and Boris Görke's labs
- GFP fusion:
- Antibody: available in Stülke lab
Labs working on this gene/protein
Stephane Aymerich, Microbiology and Molecular Genetics, INRA Paris-Grignon, France
Your additional remarks
References
Reviews
Sabine Brantl, Andreas Licht
Characterisation of Bacillus subtilis transcriptional regulators involved in metabolic processes.
Curr Protein Pept Sci: 2010, 11(4);274-91
[PubMed:20408793]
[WorldCat.org]
[DOI]
(I p)
Original Publications
Cédric Atmanene, Denix Chaix, Yannick Bessin, Nathalie Declerck, Alain Van Dorsselaer, Sarah Sanglier-Cianferani
Combination of noncovalent mass spectrometry and traveling wave ion mobility spectrometry reveals sugar-induced conformational changes of central glycolytic genes repressor/DNA complex.
Anal Chem: 2010, 82(9);3597-605
[PubMed:20361740]
[WorldCat.org]
[DOI]
(I p)
Fabian M Commichau, Fabian M Rothe, Christina Herzberg, Eva Wagner, Daniel Hellwig, Martin Lehnik-Habrink, Elke Hammer, Uwe Völker, Jörg Stülke
Novel activities of glycolytic enzymes in Bacillus subtilis: interactions with essential proteins involved in mRNA processing.
Mol Cell Proteomics: 2009, 8(6);1350-60
[PubMed:19193632]
[WorldCat.org]
[DOI]
(I p)
Pavlína Rezácová, Milan Kozísek, Shiu F Moy, Irena Sieglová, Andrzej Joachimiak, Mischa Machius, Zbyszek Otwinowski
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: 2008, 69(4);895-910
[PubMed:18554327]
[WorldCat.org]
[DOI]
(I p)
Thierry Doan, Laetitia Martin, Silvia Zorrilla, Denis Chaix, Stéphane Aymerich, Gilles Labesse, Nathalie Declerck
A phospho-sugar binding domain homologous to NagB enzymes regulates the activity of the central glycolytic genes repressor.
Proteins: 2008, 71(4);2038-50
[PubMed:18186488]
[WorldCat.org]
[DOI]
(I p)
Silvia Zorrilla, Denis Chaix, Alvaro Ortega, Carlos Alfonso, Thierry Doan, Emmanuel Margeat, Germán Rivas, Stephan Aymerich, Nathalie Declerck, Catherine A Royer
Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR).
Biochemistry: 2007, 46(51);14996-5008
[PubMed:18052209]
[WorldCat.org]
[DOI]
(P p)
Silvia Zorrilla, Thierry Doan, Carlos Alfonso, Emmanuel Margeat, Alvaro Ortega, Germán Rivas, Stéphane Aymerich, Catherine A Royer, Nathalie Declerck
Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA.
Biophys J: 2007, 92(9);3215-27
[PubMed:17293407]
[WorldCat.org]
[DOI]
(P p)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)
Christoph Meinken, Hans-Matti Blencke, Holger Ludwig, Jörg Stülke
Expression of the glycolytic gapA operon in Bacillus subtilis: differential syntheses of proteins encoded by the operon.
Microbiology (Reading): 2003, 149(Pt 3);751-761
[PubMed:12634343]
[WorldCat.org]
[DOI]
(P p)
Thierry Doan, Stéphane Aymerich
Regulation of the central glycolytic genes in Bacillus subtilis: binding of the repressor CggR to its single DNA target sequence is modulated by fructose-1,6-bisphosphate.
Mol Microbiol: 2003, 47(6);1709-21
[PubMed:12622823]
[WorldCat.org]
[DOI]
(P p)
Holger Ludwig, Nicole Rebhan, Hans-Matti Blencke, Matthias Merzbacher, Jörg Stülke
Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation.
Mol Microbiol: 2002, 45(2);543-53
[PubMed:12123463]
[WorldCat.org]
[DOI]
(P p)
H Ludwig, G Homuth, M Schmalisch, F M Dyka, M Hecker, J Stülke
Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon.
Mol Microbiol: 2001, 41(2);409-22
[PubMed:11489127]
[WorldCat.org]
[DOI]
(P p)
S Fillinger, S Boschi-Muller, S Azza, E Dervyn, G Branlant, S Aymerich
Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium.
J Biol Chem: 2000, 275(19);14031-7
[PubMed:10799476]
[WorldCat.org]
[DOI]
(P p)