Difference between revisions of "RocG"
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=Expression and regulation= | =Expression and regulation= | ||
* '''Operon:''' ''rocG'' {{PubMed|10468601}} | * '''Operon:''' ''rocG'' {{PubMed|10468601}} | ||
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+ | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rocG_3880740_3882014_-1 rocG] {{PubMed|22383849}} | ||
* '''Sigma factor:''' [[SigL]] {{PubMed|10468601}} | * '''Sigma factor:''' [[SigL]] {{PubMed|10468601}} |
Revision as of 08:49, 17 April 2012
- Description: trigger enzyme: catabolic glutamate dehydrogenase induced by arginine, ornithine or proline, subject to carbon catabolite repression
Gene name | rocG |
Synonyms | |
Essential | no |
Product | trigger enzyme: glutamate dehydrogenase (major) |
Function | arginine utilization, controls the activity of GltC |
Interactions involving this protein in SubtInteract: RocG | |
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate | |
MW, pI | 46.2 kDa, 6.28 |
Gene length, protein length | 1272 bp, 424 amino acids |
Immediate neighbours | rocA, yweA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
utilization of amino acids, transcription factors and their control, trigger enzyme
This gene is a member of the following regulons
AbrB regulon, AhrC regulon, CcpA regulon, RocR regulon, SigL regulon
The gene
Basic information
- Locus tag: BSU37790
Phenotypes of a mutant
- Poor growth on complex media such as SP (sporulation medium). No growth in minimal media with arginine as the only carbon source. Rapid accumulation of suppressor mutants (gudB1)
- sensitive to ß-lactam antibiotics such as cefuroxime and to fosfomycin (suppressed by activation of gudB) due to the downregulation of the SigW regulon PubMed
- transcription profile of a rocG gudB mutant strain: GEO PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+ (according to Swiss-Prot), controls the activity of the GltC transcription activator PubMed
- Protein family: Glu/Leu/Phe/Val dehydrogenases family (according to Swiss-Prot)
- Paralogous protein(s): GudB
Extended information on the protein
- Kinetic information: KM [glutamate] = 2.9 mM, KM [ammonium] = 18 mM PubMed
- Domains:
- Modification:
- Cofactor(s): NAD+/NADH + H+
- Effectors of protein activity:
Database entries
- Structure: 3K92 (super-repressor mutant that is capable of constitutive inactivation of GltC, E93K mutation) PubMed
- UniProt: P39633
- KEGG entry: [4]
- E.C. number: 1.4.1.2
Additional information
Expression and regulation
- Operon: rocG PubMed
- Regulation:
- Regulatory mechanism:
- Additional information:
Activation by RocR requires binding of RocR to a downstream element PubMed
Biological materials
- Mutant: GP747 (spc), GP726 (aphA3), GP810 (del tet), GP1157 (cat) all available in Stülke lab
- Expression vector:
- expression of native rocG in B. subtilis: pGP529 (in pBQ200), available in Stülke lab
- for purification of RocG from E. coli carrying an N-terminal Strep-tag: pGP902 (in pGP172), a series of rocG variants is also available in pGP172, available in Stülke lab
- for expression/ purification from E. coli with N-terminal His-tag and thrombin cleavage site, in pWH844: pGP860, available in Stülke lab
- purification from B. subtilis with an N-terminal Strep-tag, for SPINE, (in pGP380): pGP1709, available in Stülke lab
- 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
Enzymatic activity of RocG
Kenji Manabe, Yasushi Kageyama, Takuya Morimoto, Tadahiro Ozawa, Kazuhisa Sawada, Keiji Endo, Masatoshi Tohata, Katsutoshi Ara, Katsuya Ozaki, Naotake Ogasawara
Combined effect of improved cell yield and increased specific productivity enhances recombinant enzyme production in genome-reduced Bacillus subtilis strain MGB874.
Appl Environ Microbiol: 2011, 77(23);8370-81
[PubMed:21965396]
[WorldCat.org]
[DOI]
(I p)
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)
Shigeki Kada, Masahiro Yabusaki, Takayuki Kaga, Hitoshi Ashida, Ken-ichi Yoshida
Identification of two major ammonia-releasing reactions involved in secondary natto fermentation.
Biosci Biotechnol Biochem: 2008, 72(7);1869-76
[PubMed:18603778]
[WorldCat.org]
[DOI]
(I p)
Fabian M Commichau, Katrin Gunka, Jens J Landmann, Jörg Stülke
Glutamate metabolism in Bacillus subtilis: gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations of the system.
J Bacteriol: 2008, 190(10);3557-64
[PubMed:18326565]
[WorldCat.org]
[DOI]
(I p)
Md Iqbal Hassan Khan, Kousuke Ito, Hyeung Kim, Hiroyuki Ashida, Takahiro Ishikawa, Hitoshi Shibata, Yoshihiro Sawa
Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis.
Biosci Biotechnol Biochem: 2005, 69(10);1861-70
[PubMed:16244435]
[WorldCat.org]
[DOI]
(P p)
Iqbal Hassan Khan, Hyeung Kim, Hiroyuki Ashida, Takahiro Ishikawa, Hitoshi Shibata, Yoshihiro Sawa
Altering the substrate specificity of glutamate dehydrogenase from Bacillus subtilis by site-directed mutagenesis.
Biosci Biotechnol Biochem: 2005, 69(9);1802-5
[PubMed:16195607]
[WorldCat.org]
[DOI]
(P p)
B R Belitsky, A L Sonenshein
Role and regulation of Bacillus subtilis glutamate dehydrogenase genes.
J Bacteriol: 1998, 180(23);6298-305
[PubMed:9829940]
[WorldCat.org]
[DOI]
(P p)
Function in the control of GltC activity
Expression of rocG
Additional publications: PubMed
Structural analysis of glutamate dehydrogenase
Bypass of rocG mutations