Difference between revisions of "TrpA"

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* '''Additional information:'''
 
* '''Additional information:'''
 
** the mRNA is substantially stabilized upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}}
 
** the mRNA is substantially stabilized upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium): 108 {{PubMed|24696501}}
 +
** number of protein molecules per cell (complex medium with amino acids, without glucose): 656 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 09:53, 17 April 2014

  • Description: tryptophan synthase (alpha subunit)

Gene name trpA
Synonyms
Essential no
Product tryptophan synthase (alpha subunit)
Function biosynthesis of tryptophan
Gene expression levels in SubtiExpress: trpA
Interactions involving this protein in SubtInteract: TrpA
Metabolic function and regulation of this protein in SubtiPathways:
trpA
MW, pI 29 kDa, 4.817
Gene length, protein length 801 bp, 267 aa
Immediate neighbours hisC, trpB
Sequences Protein DNA DNA_with_flanks
Genetic context
TrpA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TrpA 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: BSU22630

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: UPF0403 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure: 1WQ5 (from Escherichia coli, 35% identity, 53% 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:
    • the mRNA is substantially stabilized upon depletion of RNase Y PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 108 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 656 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, 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)