Difference between revisions of "GudB"

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(Biological materials)
(Biological materials)
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** for purification of GudB from ''E. coli'' carrying an N-terminal Strep-tag: pGP863 (in [[pGP172]]) available in [[Stülke]] lab
 
** for purification of GudB from ''E. coli'' carrying an N-terminal Strep-tag: pGP863 (in [[pGP172]]) available in [[Stülke]] lab
 
** for purification of GudB1 from ''E. coli'' carrying an N-terminal Strep-tag: pGP864 (in [[pGP172]]) available in [[Stülke]] lab
 
** for purification of GudB1 from ''E. coli'' carrying an N-terminal Strep-tag: pGP864 (in [[pGP172]]) available in [[Stülke]] lab
** for ectopic expression of ''gudB'' with its native promoter: pGP900 (in [[pAC5]]), available in [[Stülke]] lab      
+
** for ectopic expression of ''gudB'' with its native promoter: pGP900 (in [[pAC5]]), available in [[Stülke]] lab
 +
** wild type ''gudB'', expression in ''B. subtilis'', in pBQ200: pGP1712, available in [[Stülke]] lab       
 
* '''lacZ fusion:''' pGP651 (in [[pAC5]]), available in [[Stülke]] lab
 
* '''lacZ fusion:''' pGP651 (in [[pAC5]]), available in [[Stülke]] lab
  

Revision as of 07:33, 31 March 2011

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

Gene name gudB
Synonyms ypcA
Essential no
Product trigger enzyme: glutamate dehydrogenase
Function glutamate utilization, control of GltC activity
Metabolic function and regulation of this protein in SubtiPathways:
Ammonium/ glutamate
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







Categories containing this gene/protein

utilization of amino acids, trigger enzyme

This gene is a member of the following regulons

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: 3K8Z (enzymatically active GudB1) PubMed
  • 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), GP1160 (del aphA3) both available in Stülke lab
  • Expression vector:
    • for purification of GudB from E. coli carrying an N-terminal Strep-tag: pGP863 (in pGP172) available in Stülke lab
    • for purification of GudB1 from E. coli carrying an N-terminal Strep-tag: pGP864 (in pGP172) available in Stülke lab
    • for ectopic expression of gudB with its native promoter: pGP900 (in pAC5), available in Stülke lab
    • wild type gudB, expression in B. subtilis, in pBQ200: pGP1712, available in Stülke lab
  • lacZ fusion: pGP651 (in pAC5), available in Stülke lab
  • FLAG-tag construct: GP1194 (gudB, spc, based on pGP1331), GP1195 (gudB1, spc, based on pGP1331), 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