Difference between revisions of "GltC"
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=References= | =References= | ||
==Reviews== | ==Reviews== | ||
− | <pubmed> 20408793 | + | <big>''Gunka K, Commichau FM'' </big> |
+ | <big>'''Control of glutamate homeostasis in ''Bacillus subtilis'':''' </big> | ||
+ | <big>'''a complex interplay between ammonium assimilation, glutamate biosynthesis and degradation. ''' </big> | ||
+ | <big>Mol Microbiol.: 2012, 85(2) 213-224. </big> | ||
+ | [http://www.ncbi.nlm.nih.gov/pubmed/22625175 PubMed:22625175] | ||
+ | <pubmed> 20408793 </pubmed> | ||
+ | |||
==Original Publications== | ==Original Publications== | ||
<pubmed>7559360 15150225 2548995 17183217 17608797 17134717 14523131, 20630473</pubmed> | <pubmed>7559360 15150225 2548995 17183217 17608797 17134717 14523131, 20630473</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 17:42, 6 July 2012
- Description: Transcriptional activator of the gltA-gltB operon. Activates expression of the operon in the absence of arginine.
Gene name | gltC |
Synonyms | |
Essential | No |
Product | transcriptional regulator (LysR family) |
Function | positive regulation of the glutamate synthase operon (gltAB) |
Interactions involving this protein in SubtInteract: GltC | |
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate | |
MW, pI | 33.9 kDa, 5.62 |
Gene length, protein length | 900 bp, 300 amino acids |
Immediate neighbours | gltA, proJ |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, glutamate metabolism, transcription factors and their control
This gene is a member of the following regulons
The GltC regulon:
The gene
Basic information
- Locus tag: BSU18460
Phenotypes of a mutant
gltC mutants are auxotrophic for glutamate.
Database entries
- DBTBS entry: [1]
- SubtiList entry:[2]
Additional information
The protein
Basic information/ Evolution
- Protein family: LysR family PubMed
- Paralogous protein(s): none, but there are 19 members of the LysR family in B. subtilis
Extended information on the protein
- Kinetic information:
- Domains: DNA-binding helix-turn-helix motif: AA 18 ... 37
- Modification:
- Cofactor(s):
- Effectors of protein activity: 2-oxoglutarate stimulates transcription activation, glutamate inhibits transcription activation PubMed
Database entries
- Structure:
- UniProt: P20668
- KEGG entry: [3]
Additional information
Expression and regulation
- Regulation: autoregulation by GltC PubMed
- Regulatory mechanism: autorepression PubMed
- Database entries: DBTBS
- Additional information:
Biological materials
- Mutant: GP344 (erm), GP738 (spc) (available in Stülke lab)
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody: available in Stülke lab
Labs working on this gene/protein
Linc Sonenshein, Tufts University, Boston, MA, USA Homepage
Jörg Stülke, University of Göttingen, Germany Homepage
Fabian Commichau University of Göttingen, Germany Homepage
Your additional remarks
References
Reviews
Gunka K, Commichau FM Control of glutamate homeostasis in Bacillus subtilis: a complex interplay between ammonium assimilation, glutamate biosynthesis and degradation. Mol Microbiol.: 2012, 85(2) 213-224. PubMed:22625175
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
Katrin Gunka, Joseph A Newman, Fabian M Commichau, Christina Herzberg, Cecilia Rodrigues, Lorraine Hewitt, Richard J Lewis, Jörg Stülke
Functional dissection of a trigger enzyme: mutations of the bacillus subtilis glutamate dehydrogenase RocG that affect differentially its catalytic activity and regulatory properties.
J Mol Biol: 2010, 400(4);815-27
[PubMed:20630473]
[WorldCat.org]
[DOI]
(I p)
Fabian M Commichau, Christina Herzberg, Philipp Tripal, Oliver Valerius, Jörg Stülke
A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: the glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC.
Mol Microbiol: 2007, 65(3);642-54
[PubMed:17608797]
[WorldCat.org]
[DOI]
(P p)
Fabian M Commichau, Ingrid Wacker, Jan Schleider, Hans-Matti Blencke, Irene Reif, Philipp Tripal, Jörg Stülke
Characterization of Bacillus subtilis mutants with carbon source-independent glutamate biosynthesis.
J Mol Microbiol Biotechnol: 2007, 12(1-2);106-13
[PubMed:17183217]
[WorldCat.org]
[DOI]
(P p)
Silvia Picossi, Boris R Belitsky, Abraham L Sonenshein
Molecular mechanism of the regulation of Bacillus subtilis gltAB expression by GltC.
J Mol Biol: 2007, 365(5);1298-313
[PubMed:17134717]
[WorldCat.org]
[DOI]
(P p)
Boris R Belitsky, Abraham L Sonenshein
Modulation of activity of Bacillus subtilis regulatory proteins GltC and TnrA by glutamate dehydrogenase.
J Bacteriol: 2004, 186(11);3399-407
[PubMed:15150225]
[WorldCat.org]
[DOI]
(P p)
Ingrid Wacker, Holger Ludwig, Irene Reif, Hans-Matti Blencke, Christian Detsch, Jörg Stülke
The regulatory link between carbon and nitrogen metabolism in Bacillus subtilis: regulation of the gltAB operon by the catabolite control protein CcpA.
Microbiology (Reading): 2003, 149(Pt 10);3001-3009
[PubMed:14523131]
[WorldCat.org]
[DOI]
(P p)
B R Belitsky, A L Sonenshein
Mutations in GltC that increase Bacillus subtilis gltA expression.
J Bacteriol: 1995, 177(19);5696-700
[PubMed:7559360]
[WorldCat.org]
[DOI]
(P p)
D E Bohannon, A L Sonenshein
Positive regulation of glutamate biosynthesis in Bacillus subtilis.
J Bacteriol: 1989, 171(9);4718-27
[PubMed:2548995]
[WorldCat.org]
[DOI]
(P p)