Difference between revisions of "LeuA"

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* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/1577690 PubMed]
 
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/1577690 PubMed]
  
−
* '''Regulation:''' repressed by casamino acids [http://www.ncbi.nlm.nih.gov/pubmed/12107147 PubMed] ,  expressed in the absence of branched-chain amino acids (BCAA), expression is stimulated in the presence of glucose [http://www.ncbi.nlm.nih.gov/sites/entrez/12193635 PubMed], repressed by [[CodY]] [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed]
+
* '''Regulation:''' for a complete overview on the regulation of the ilv operon, see [http://www.ncbi.nlm.nih.gov/pubmed/20935095 Brinsmade ''et al''.]
 +
** repressed by casamino acids [http://www.ncbi.nlm.nih.gov/pubmed/12107147 PubMed]  
 +
** expression is stimulated in the presence of glucose [http://www.ncbi.nlm.nih.gov/sites/entrez/12193635 PubMed]  
 
** repressed in the absence of good nitrogen sources (glutamine or ammonium) ([[TnrA]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/15547269 PubMed]
 
** repressed in the absence of good nitrogen sources (glutamine or ammonium) ([[TnrA]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/15547269 PubMed]
−
** repressed during growth in the presence of branched chain amino acids ([[CodY]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed]
+
** repressed during growth in the presence of branched chain amino acids ([[CodY]], [[T-box]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed]
  
−
* '''Regulatory mechanism:''' [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed], glucose regulation: [[CcpA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/12193635 PubMed], repression by BCAA: tRNA-controlled RNA switch (T-box) that mediates termination/antitermination
+
* '''Regulatory mechanism:'''  
 +
** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed]  
 +
** [[CcpA]]: transcription activation [http://www.ncbi.nlm.nih.gov/sites/entrez/12193635 PubMed]
 +
** [[T-box]]: tRNA-controlled [[RNA switch]] that mediates termination/antitermination
 
** [[TnrA]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/15547269 PubMed]
 
** [[TnrA]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/15547269 PubMed]
−
** [[CodY]]: transcription repression [http://www.ncbi.nlm.nih.gov/sites/entrez/12618455 PubMed]
 
  
 
* '''Additional information:''' subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
 
* '''Additional information:''' subject to Clp-dependent proteolysis upon glucose starvation [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+17981983 PubMed]
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=References=
 
=References=
  
−
<pubmed>15060025,12193635,19258532,8289305,18641142,15547269,12618455,,15547269,12618455,12107147 18763711, </pubmed>
+
<pubmed>15060025,12193635,19258532,8289305,18641142,15547269,12618455,,15547269,12618455,12107147 18763711, 20935095</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:36, 26 October 2010

  • Description: 2-isopropylmalate synthase

Gene name leuA
Synonyms
Essential no
Product 2-isopropylmalate synthase
Function biosynthesis of leucine
Metabolic function and regulation of this protein in SubtiPathways:
Ile, Leu, Val, Coenzyme A
MW, pI 56 kDa, 5.657
Gene length, protein length 1554 bp, 518 aa
Immediate neighbours leuB, ilvC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
LeuA context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU28280

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate + CoA (according to Swiss-Prot)
  • Protein family: LeuA type 1 subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot), membrane PubMed

Database entries

  • Structure: 3EEG (from Cytophaga hutchinsonii atcc 33406, 53% identity, 68% similarity)
  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation: for a complete overview on the regulation of the ilv operon, see Brinsmade et al.
    • repressed by casamino acids PubMed
    • expression is stimulated in the presence of glucose PubMed
    • repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
    • repressed during growth in the presence of branched chain amino acids (CodY, T-box) PubMed
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Shaun R Brinsmade, Roelco J Kleijn, Uwe Sauer, Abraham L Sonenshein
Regulation of CodY activity through modulation of intracellular branched-chain amino acid pools.
J Bacteriol: 2010, 192(24);6357-68
[PubMed:20935095] [WorldCat.org] [DOI] (I p)

Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Shigeo Tojo, Takenori Satomura, Kanako Kumamoto, Kazutake Hirooka, Yasutaro Fujita
Molecular mechanisms underlying the positive stringent response of the Bacillus subtilis ilv-leu operon, involved in the biosynthesis of branched-chain amino acids.
J Bacteriol: 2008, 190(18);6134-47
[PubMed:18641142] [WorldCat.org] [DOI] (I p)

Shigeo Tojo, Takenori Satomura, Kaori Morisaki, Ken-Ichi Yoshida, Kazutake Hirooka, Yasutaro Fujita
Negative transcriptional regulation of the ilv-leu operon for biosynthesis of branched-chain amino acids through the Bacillus subtilis global regulator TnrA.
J Bacteriol: 2004, 186(23);7971-9
[PubMed:15547269] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Susanne Hennig, Michael Hecker, Georg Homuth
Transcriptional organization and posttranscriptional regulation of the Bacillus subtilis branched-chain amino acid biosynthesis genes.
J Bacteriol: 2004, 186(8);2240-52
[PubMed:15060025] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

Holger Ludwig, Christoph Meinken, Anastasija Matin, Jörg Stülke
Insufficient expression of the ilv-leu operon encoding enzymes of branched-chain amino acid biosynthesis limits growth of a Bacillus subtilis ccpA mutant.
J Bacteriol: 2002, 184(18);5174-8
[PubMed:12193635] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

F J Grundy, T M Henkin
Conservation of a transcription antitermination mechanism in aminoacyl-tRNA synthetase and amino acid biosynthesis genes in gram-positive bacteria.
J Mol Biol: 1994, 235(2);798-804
[PubMed:8289305] [WorldCat.org] [DOI] (P p)

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