Difference between revisions of "GudB"

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=References=
 
=References=
  
<pubmed>17183217 18723616, </pubmed>
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<pubmed>18603778,,17183217 18723616, </pubmed>
 
# Belitsky BR, Sonenshein AL (1998) Role and regulation of Bacillus subtilis glutamate dehydrogenase genes. J Bacteriol 180:6298-6305 [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+9829940 PubMed]
 
# Belitsky BR, Sonenshein AL (1998) Role and regulation of Bacillus subtilis glutamate dehydrogenase genes. J Bacteriol 180:6298-6305 [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+9829940 PubMed]
 
# Commichau, F. M., Wacker, I., Schleider, J., Blencke, H.-M., Reif, I., Tripal, P., and Stülke, J. (2007) Characterization of ''Bacillus subtilis'' mutants with carbon source-independent glutamate biosynthesis. J Mol Microbiol Biotechnol 12: 106-113. [http://www.ncbi.nlm.nih.gov/sites/entrez/17183217 PubMed]
 
# Commichau, F. M., Wacker, I., Schleider, J., Blencke, H.-M., Reif, I., Tripal, P., and Stülke, J. (2007) Characterization of ''Bacillus subtilis'' mutants with carbon source-independent glutamate biosynthesis. J Mol Microbiol Biotechnol 12: 106-113. [http://www.ncbi.nlm.nih.gov/sites/entrez/17183217 PubMed]

Revision as of 10:45, 14 June 2009

  • Description: trigger enzyme: glutamate dehydrogenase (cryptic in 168 and derivatives)

Gene name gudB
Synonyms ypcA
Essential no
Product glutamate dehydrogenase
Function glutamate utilization, control of GltC activity
MW, pI 47 kDa, 5.582
Gene length, protein length 1278 bp, 426 aa
Immediate neighbours ypdA, ypbH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
GudB context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU22960

Phenotypes of a mutant

The gene is cryptic. If gudB is activated (gudB1 mutation), the bacteria are able to utilize glutamate as the only carbon source. 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 (according to Swiss-Prot)
  • Protein family: Glu/Leu/Phe/Val dehydrogenases family (according to Swiss-Prot)
  • Paralogous protein(s): RocG

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation: constitutively expressed
  • Regulatory mechanism:
  • Additional information: GudB is subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant: GP691 (cat), available in Stülke lab
  • Expression vector:
  • lacZ fusion: pGP651 (in pAC5), available in Stülke lab
  • GFP fusion:
  • two-hybrid system:
  • Antibody: antibody against RocG recognizes GudB, 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

The GudB protein is active in other legacy B. subtilis strains (e.g. strain 122). Thus, it can be speculated that the ancestral gudB gene was not cryptic, but became so as a product of the "domestication" of B. subtilis 168 in the lab. PubMed

References

Daniel R Zeigler, Zoltán Prágai, Sabrina Rodriguez, Bastien Chevreux, Andrea Muffler, Thomas Albert, Renyuan Bai, Markus Wyss, John B Perkins
The origins of 168, W23, and other Bacillus subtilis legacy strains.
J Bacteriol: 2008, 190(21);6983-95
[PubMed:18723616] [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, 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)

  1. Belitsky BR, Sonenshein AL (1998) Role and regulation of Bacillus subtilis glutamate dehydrogenase genes. J Bacteriol 180:6298-6305 PubMed
  2. Commichau, F. M., Wacker, I., Schleider, J., Blencke, H.-M., Reif, I., Tripal, P., and Stülke, J. (2007) Characterization of Bacillus subtilis mutants with carbon source-independent glutamate biosynthesis. J Mol Microbiol Biotechnol 12: 106-113. PubMed
  3. Commichau, F. M., Gunka, K., Landmann, J. J. & Stülke, J. (2008) Glutamate metabolism in Bacillus subtilis: Gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations in the system. J. Bacteriol. 190: 3557-3564. PubMed
  4. Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
  5. Zeigler DR, Prágai Z, Rodriguez S, Chevreux B, Muffler A, Albert T, Bai R, Wyss M, Perkins JB (2008) The origins of 168, W23, and other Bacillus subtilis legacy strains. J Bacteriol 190(21):6983-95 PubMed
  6. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed