Difference between revisions of "TrpE"

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(The trpE RNA switch)
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<pubmed>19385727, ,16285852 </pubmed>
 
<pubmed>19385727, ,16285852 </pubmed>
 
==The ''trpE'' [[RNA switch]]==
 
==The ''trpE'' [[RNA switch]]==
<pubmed> 20384694 19033375, 17881743, 7515880,2422155,3133360, 7678334,7592410, 14976255, 2422155,8419914, 1551827, 16285852 10714985 11566991 12963367 14712717 21097886 24505391 </pubmed>
+
<pubmed> 20384694 19033375, 17881743, 7515880,2422155,3133360, 7678334,7592410, 14976255, 2422155,8419914, 1551827, 16285852 10714985 11566991 12963367 14712717 21097886 24505391 24682818</pubmed>
  
 
==Other original publications==
 
==Other original publications==
 
<pubmed> 4956345 3924737, 6436812, 21815947  </pubmed>
 
<pubmed> 4956345 3924737, 6436812, 21815947  </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:35, 2 April 2014

  • Description: anthranilate synthase (subunit I)

Gene name trpE
Synonyms
Essential no
Product anthranilate synthase (subunit I)
Function biosynthesis of tryptophan
Gene expression levels in SubtiExpress: trpE
Interactions involving this protein in SubtInteract: TrpE
Metabolic function and regulation of this protein in SubtiPathways:
trpE
MW, pI 57 kDa, 5.246
Gene length, protein length 1545 bp, 515 aa
Immediate neighbours trpD, aroH
Sequences Protein DNA DNA_with_flanks
Genetic context
TrpE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TrpE expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

TRAP regulon

The gene

Basic information

  • Locus tag: BSU22680

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity: subject to feedback inhibtion by tryptophan PubMed

Database entries

  • Structure: 1I7Q (from Serratia marcescens, 42% identity, 62% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism:
    • TRAP: binding to the mRNA in the presence of tryptophan, this results in transcription termination PubMed
  • Additional information:
    • subject to feedback inhibtion by tryptophan PubMed
    • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Paul Babitzke, Carol S Baker, Tony Romeo
Regulation of translation initiation by RNA binding proteins.
Annu Rev Microbiol: 2009, 63;27-44
[PubMed:19385727] [WorldCat.org] [DOI] (I p)

Paul Gollnick, Paul Babitzke, Alfred Antson, Charles Yanofsky
Complexity in regulation of tryptophan biosynthesis in Bacillus subtilis.
Annu Rev Genet: 2005, 39;47-68
[PubMed:16285852] [WorldCat.org] [DOI] (P p)

The trpE RNA switch


Other original publications

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

D J Henner, L Band, H Shimotsu
Nucleotide sequence of the Bacillus subtilis tryptophan operon.
Gene: 1985, 34(2-3);169-77
[PubMed:3924737] [WorldCat.org] [DOI] (P p)

H Shimotsu, D J Henner
Characterization of the Bacillus subtilis tryptophan promoter region.
Proc Natl Acad Sci U S A: 1984, 81(20);6315-9
[PubMed:6436812] [WorldCat.org] [DOI] (P p)

E W Nester, R A Jensen
Control of aromatic acid biosynthesis in Bacillus subtilis: sequenial feedback inhibition.
J Bacteriol: 1966, 91(4);1594-8
[PubMed:4956345] [WorldCat.org] [DOI] (P p)