Difference between revisions of "TrpB"

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(Original publications)
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<pubmed> 18486479 11893063 11163353 7900177 19387555 </pubmed>
 
<pubmed> 18486479 11893063 11163353 7900177 19387555 </pubmed>
 
==Original publications==
 
==Original publications==
<big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J''  </big>
+
<pubmed> 14976255, 3924737, 6436812,2422155,8419914, 1551827, 17507374 21815947 </pubmed>
<big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big>
 
<big>Mol Microbiol. 2011 81(6): 1459-1473. </big>
 
[http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947]
 
<pubmed> 14976255, 3924737, 6436812,2422155,8419914, 1551827, 17507374  </pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:23, 13 July 2013

  • Description: tryptophan synthase (beta subunit)

Gene name trpB
Synonyms
Essential no
Product tryptophan synthase (beta subunit)
Function biosynthesis of tryptophan
Gene expression levels in SubtiExpress: trpB
Interactions involving this protein in SubtInteract: TrpB
Metabolic function and regulation of this protein in SubtiPathways:
Phe, Tyr, Trp
MW, pI 43 kDa, 5.526
Gene length, protein length 1200 bp, 400 aa
Immediate neighbours trpA, trpF
Sequences Protein DNA DNA_with_flanks
Genetic context
TrpB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
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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: BSU22640

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
    • TRAP: binding to the mRNA in the presence of tryptophan, this results in transcription termination PubMed
  • Additional information:
    • 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

Samanta Raboni, Stefano Bettati, Andrea Mozzarelli
Tryptophan synthase: a mine for enzymologists.
Cell Mol Life Sci: 2009, 66(14);2391-403
[PubMed:19387555] [WorldCat.org] [DOI] (I p)

Michael F Dunn, Dimitri Niks, Huu Ngo, Thomas R M Barends, Ilme Schlichting
Tryptophan synthase: the workings of a channeling nanomachine.
Trends Biochem Sci: 2008, 33(6);254-64
[PubMed:18486479] [WorldCat.org] [DOI] (P p)

E W Miles
Tryptophan synthase: a multienzyme complex with an intramolecular tunnel.
Chem Rec: 2001, 1(2);140-51
[PubMed:11893063] [WorldCat.org] [DOI] (P p)

N K Nagradova
Interdomain interactions in oligomeric enzymes: creation of asymmetry in homo-oligomers and role in metabolite channeling between active centers of hetero-oligomers.
FEBS Lett: 2001, 487(3);327-32
[PubMed:11163353] [WorldCat.org] [DOI] (P p)

E W Miles
Tryptophan synthase. Structure, function, and protein engineering.
Subcell Biochem: 1995, 24;207-54
[PubMed:7900177] [WorldCat.org] (P p)

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)

Gintaras Deikus, David H Bechhofer
Initiation of decay of Bacillus subtilis trp leader RNA.
J Biol Chem: 2007, 282(28);20238-44
[PubMed:17507374] [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)

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, 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)

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)

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)