Difference between revisions of "RocG"

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=== Database entries ===
 
=== Database entries ===
  
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* '''Structure:''' [http://www.rcsb.org/pdb/search/structidSearch.do?structureId=3K92 3K92] (super-repressor mutant that is capable of constitutive inactivation of [[GltC]], E93K mutation)
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* '''Structure:''' [http://www.rcsb.org/pdb/search/structidSearch.do?structureId=3K92 3K92] (super-repressor mutant that is capable of constitutive inactivation of [[GltC]], E93K mutation) {{PubMed|20630473}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39633 P39633]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P39633 P39633]
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'''Enzymatic activity of RocG'''
 
'''Enzymatic activity of RocG'''
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<pubmed>18603778,,16244435 16195607 ,18326565, 9829940  </pubmed>
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<pubmed>18603778,,16244435 16195607 ,18326565, 9829940 20630473 </pubmed>
 
   
 
   
 
'''Function in the control of [[GltC]] activity'''
 
'''Function in the control of [[GltC]] activity'''
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<pubmed>15150225,17994626 ,17608797 17183217  </pubmed>
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<pubmed>15150225,17994626 ,17608797 17183217 20630473   </pubmed>
  
 
'''Expression of ''rocG'''''
 
'''Expression of ''rocG'''''
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'''Structural analysis of glutamate dehydrogenase'''
 
'''Structural analysis of glutamate dehydrogenase'''
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<pubmed>8263917 </pubmed>
+
<pubmed>8263917 20630473 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 19:30, 16 July 2010

  • 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
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
RocG context.gif
This image was kindly provided by SubtiList








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)

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 (according to Swiss-Prot) L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate + NH(3) + NADH, controls the activity of the GltC transcription activator PubMed
  • Protein family: Glu/Leu/Phe/Val dehydrogenases family (according to Swiss-Prot) Glu/Leu/Phe/Val dehydrogenases family
  • Paralogous protein(s): GudB

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions: RocG-GltC, this interaction prevents transcription activation of the gltA-gltB operon by GltC PubMed
  • Localization:

Database entries

  • Structure: 3K92 (super-repressor mutant that is capable of constitutive inactivation of GltC, E93K mutation) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Additional information:

Activation by RocR requires binding of RocR to a downstream element PubMed

Biological materials

  • Mutant: GP747 (spc), GP726 (aphA3), GP810 (tet) available in Stülke lab
  • Expression vector:
    • expression of native rocG in B. subtilis: pGP529 (in pBQ200), available in Stülke lab
    • for purification of RocG carrying an N-terminal Strep-tag: pGP902 (in pGP172), a series of rocG variants is also available in pGP172, 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

Your additional remarks

References

Enzymatic activity of RocG

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

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)

Christina Herzberg, Lope Andrés Flórez Weidinger, Bastian Dörrbecker, Sebastian Hübner, Jörg Stülke, Fabian M Commichau
SPINE: a method for the rapid detection and analysis of protein-protein interactions in vivo.
Proteomics: 2007, 7(22);4032-5
[PubMed:17994626] [WorldCat.org] [DOI] (P 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)

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)


Expression of rocG


Structural analysis of glutamate dehydrogenase

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