Difference between revisions of "TrpE"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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=== Additional information===
 
=== Additional information===
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=The protein=
 
=The protein=
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* '''Kinetic information:'''
 
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* '''Modification:'''
 
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* '''Effectors of protein activity:''' subject to feedback inhibtion by tryptophan {{PubMed|4956345}}  
 
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=trpE_2375869_2377416_-1 trpE] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=trpE_2375869_2377416_-1 trpE] {{PubMed|22383849}}
  
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** ''[[trpE]]'': [[SigA]] {{PubMed|6436812}}
 
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<pubmed>19385727, ,16285852 </pubmed>
 
<pubmed>19385727, ,16285852 </pubmed>
 
==The ''trpE'' [[RNA switch]]==
 
==The ''trpE'' [[RNA switch]]==
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<pubmed> 20384694 19033375, 17881743, 7515880,2422155,3133360, 7678334,7592410, 14976255, 2422155,8419914, 1551827, 16285852 10714985 11566991 12963367 14712717 21097886 </pubmed>
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<pubmed> 20384694 19033375, 17881743, 7515880,2422155,3133360, 7678334,7592410, 14976255, 2422155,8419914, 1551827, 16285852 10714985 11566991 12963367 14712717 21097886 24505391 </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 17:32, 9 February 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

Natalie M McAdams, Paul Gollnick
The Bacillus subtilis TRAP protein can induce transcription termination in the leader region of the tryptophan biosynthetic (trp) operon independent of the trp attenuator RNA.
PLoS One: 2014, 9(2);e88097
[PubMed:24505391] [WorldCat.org] [DOI] (I e)

Kristine D Potter, Natalie M Merlino, Timothy Jacobs, Paul Gollnick
TRAP binding to the Bacillus subtilis trp leader region RNA causes efficient transcription termination at a weak intrinsic terminator.
Nucleic Acids Res: 2011, 39(6);2092-102
[PubMed:21097886] [WorldCat.org] [DOI] (I p)

Alexander V Yakhnin, Paul Babitzke
Mechanism of NusG-stimulated pausing, hairpin-dependent pause site selection and intrinsic termination at overlapping pause and termination sites in the Bacillus subtilis trp leader.
Mol Microbiol: 2010, 76(3);690-705
[PubMed:20384694] [WorldCat.org] [DOI] (I p)

Adam P McGraw, Ali Mokdad, François Major, Philip C Bevilacqua, Paul Babitzke
Molecular basis of TRAP-5'SL RNA interaction in the Bacillus subtilis trp operon transcription attenuation mechanism.
RNA: 2009, 15(1);55-66
[PubMed:19033375] [WorldCat.org] [DOI] (I p)

Adam P McGraw, Philip C Bevilacqua, Paul Babitzke
TRAP-5' stem loop interaction increases the efficiency of transcription termination in the Bacillus subtilis trpEDCFBA operon leader region.
RNA: 2007, 13(11);2020-33
[PubMed:17881743] [WorldCat.org] [DOI] (P 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)

Gintaras Deikus, Paul Babitzke, David H Bechhofer
Recycling of a regulatory protein by degradation of the RNA to which it binds.
Proc Natl Acad Sci U S A: 2004, 101(9);2747-51
[PubMed:14976255] [WorldCat.org] [DOI] (P p)

Paul Babitzke, Janell Schaak, Alexander V Yakhnin, Philip C Bevilacqua
Role of RNA structure in transcription attenuation in Bacillus subtilis: the trpEDCFBA operon as a model system.
Methods Enzymol: 2003, 371;392-404
[PubMed:14712717] [WorldCat.org] [DOI] (P p)

Janell E Schaak, Helen Yakhnin, Philip C Bevilacqua, Paul Babitzke
A Mg2+-dependent RNA tertiary structure forms in the Bacillus subtilis trp operon leader transcript and appears to interfere with trpE translation control by inhibiting TRAP binding.
J Mol Biol: 2003, 332(3);555-74
[PubMed:12963367] [WorldCat.org] [DOI] (P p)

H Yakhnin, J E Babiarz, A V Yakhnin, P Babitzke
Expression of the Bacillus subtilis trpEDCFBA operon is influenced by translational coupling and Rho termination factor.
J Bacteriol: 2001, 183(20);5918-26
[PubMed:11566991] [WorldCat.org] [DOI] (P p)

H Du, A V Yakhnin, S Dharmaraj, P Babitzke
trp RNA-binding attenuation protein-5' stem-loop RNA interaction is required for proper transcription attenuation control of the Bacillus subtilis trpEDCFBA operon.
J Bacteriol: 2000, 182(7);1819-27
[PubMed:10714985] [WorldCat.org] [DOI] (P p)

E Merino, P Babitzke, C Yanofsky
trp RNA-binding attenuation protein (TRAP)-trp leader RNA interactions mediate translational as well as transcriptional regulation of the Bacillus subtilis trp operon.
J Bacteriol: 1995, 177(22);6362-70
[PubMed:7592410] [WorldCat.org] [DOI] (P p)

P Babitzke, J T Stults, S J Shire, C Yanofsky
TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a multisubunit complex that appears to recognize G/UAG repeats in the trpEDCFBA and trpG transcripts.
J Biol Chem: 1994, 269(24);16597-604
[PubMed:7515880] [WorldCat.org] (P p)

J Otridge, P Gollnick
MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner.
Proc Natl Acad Sci U S A: 1993, 90(1);128-32
[PubMed:8419914] [WorldCat.org] [DOI] (P p)

P Babitzke, C Yanofsky
Reconstitution of Bacillus subtilis trp attenuation in vitro with TRAP, the trp RNA-binding attenuation protein.
Proc Natl Acad Sci U S A: 1993, 90(1);133-7
[PubMed:7678334] [WorldCat.org] [DOI] (P p)

P Babitzke, P Gollnick, C Yanofsky
The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis.
J Bacteriol: 1992, 174(7);2059-64
[PubMed:1551827] [WorldCat.org] [DOI] (P p)

M I Kuroda, D Henner, C Yanofsky
cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon.
J Bacteriol: 1988, 170(7);3080-8
[PubMed:3133360] [WorldCat.org] [DOI] (P p)

H Shimotsu, M I Kuroda, C Yanofsky, D J Henner
Novel form of transcription attenuation regulates expression the Bacillus subtilis tryptophan operon.
J Bacteriol: 1986, 166(2);461-71
[PubMed:2422155] [WorldCat.org] [DOI] (P p)


Other original publications

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