Difference between revisions of "LysC"

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** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 1459 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 1459 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4406 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1282 {{PubMed|21395229}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 806 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 14:09, 17 April 2014

  • Description: aspartokinase II (alpha and beta subunits)

Gene name lysC
Synonyms ask, aecA
Essential no
Product aspartokinase II (alpha and beta subunits)
Function biosynthesis of lysine
Gene expression levels in SubtiExpress: lysC
Metabolic function and regulation of this protein in SubtiPathways:
lysC
MW, pI 43 kDa, 4.643
Gene length, protein length 1224 bp, 408 aa
Immediate neighbours yslB, uvrC
Sequences Protein DNA DNA_with_flanks
Genetic context
LysC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
LysC expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, most abundant proteins

This gene is a member of the following regulons

L-box

The gene

Basic information

  • Locus tag: BSU28470

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + L-aspartate = ADP + 4-phospho-L-aspartate (according to Swiss-Prot)
  • Protein family: aspartokinase family (according to Swiss-Prot)
  • Paralogous protein(s): DapG

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 2RE1 (from Neisseria meningitidis mc58, 40% identity, 58% similarity)
  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed, also degraded upon ammonium or amino acid starvation PubMed

Expression and regulation

  • Regulation:
    • repressed in the presence of lysine (L-box) PubMed
    • expression activated by glucose (5.4 fold) PubMed
    • repressed by casamino acids PubMed
  • Regulatory mechanism:
    • L-box: a riboswich that mediates transcription terimnation antitermination control PubMed
  • Additional information:
    • subject to Clp-dependent proteolysis upon glucose starvation PubMed, also degraded upon ammonium or amino acid starvation PubMed
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1459 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4406 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1282 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 806 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

Chien-Chi Lo, Carol A Bonner, Gary Xie, Mark D'Souza, Roy A Jensen
Cohesion group approach for evolutionary analysis of aspartokinase, an enzyme that feeds a branched network of many biochemical pathways.
Microbiol Mol Biol Rev: 2009, 73(4);594-651
[PubMed:19946135] [WorldCat.org] [DOI] (I p)

Original Publications

The L-box riboswitch

Larry R Fiegland, Andrew D Garst, Robert T Batey, David J Nesbitt
Single-molecule studies of the lysine riboswitch reveal effector-dependent conformational dynamics of the aptamer domain.
Biochemistry: 2012, 51(45);9223-33
[PubMed:23067368] [WorldCat.org] [DOI] (I p)

Sharnise N Wilson-Mitchell, Frank J Grundy, Tina M Henkin
Analysis of lysine recognition and specificity of the Bacillus subtilis L box riboswitch.
Nucleic Acids Res: 2012, 40(12);5706-17
[PubMed:22416067] [WorldCat.org] [DOI] (I p)

Simon Blouin, Raja Chinnappan, Daniel A Lafontaine
Folding of the lysine riboswitch: importance of peripheral elements for transcriptional regulation.
Nucleic Acids Res: 2011, 39(8);3373-87
[PubMed:21169337] [WorldCat.org] [DOI] (I p)

Trang Thi Phuong Phan, Wolfgang Schumann
Transcriptional analysis of the lysine-responsive and riboswitch-regulated lysC gene of Bacillus subtilis.
Curr Microbiol: 2009, 59(4);463-8
[PubMed:19636616] [WorldCat.org] [DOI] (I p)

Narasimhan Sudarsan, J Kenneth Wickiser, Shingo Nakamura, Margaret S Ebert, Ronald R Breaker
An mRNA structure in bacteria that controls gene expression by binding lysine.
Genes Dev: 2003, 17(21);2688-97
[PubMed:14597663] [WorldCat.org] [DOI] (P p)

Frank J Grundy, Susan C Lehman, Tina M Henkin
The L box regulon: lysine sensing by leader RNAs of bacterial lysine biosynthesis genes.
Proc Natl Acad Sci U S A: 2003, 100(21);12057-62
[PubMed:14523230] [WorldCat.org] [DOI] (P p)


Other original Publications

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [WorldCat.org] [DOI] (I p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [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)

Y Lu, T N Shevtchenko, H Paulus
Fine-structure mapping of cis-acting control sites in the lysC operon of Bacillus subtilis.
FEMS Microbiol Lett: 1992, 71(1);23-7
[PubMed:1624109] [WorldCat.org] [DOI] (P p)

L M Graves, R L Switzer
Aspartokinase II from Bacillus subtilis is degraded in response to nutrient limitation.
J Biol Chem: 1990, 265(25);14947-55
[PubMed:2168395] [WorldCat.org] (P p)

N Y Chen, J J Zhang, H Paulus
Chromosomal location of the Bacillus subtilis aspartokinase II gene and nucleotide sequence of the adjacent genes homologous to uvrC and trx of Escherichia coli.
J Gen Microbiol: 1989, 135(11);2931-40
[PubMed:2559145] [WorldCat.org] [DOI] (P p)

M Petricek, L Rutberg, L Hederstedt
The structural gene for aspartokinase II in Bacillus subtilis is closely linked to the sdh operon.
FEMS Microbiol Lett: 1989, 52(1-2);85-7
[PubMed:2557260] [WorldCat.org] [DOI] (P p)