AcoL

From SubtiWiki
Revision as of 14:02, 17 April 2014 by 134.76.70.252 (talk)
Jump to: navigation, search
  • Description: acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase)

Gene name acoL
Synonyms yfjH
Essential no
Product acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase)
Function acetoin utilization
Gene expression levels in SubtiExpress: acoL
Interactions involving this protein in SubtInteract: AcoL
Metabolic function and regulation of this protein in SubtiPathways:
acoL
MW, pI 48 kDa, 5.273
Gene length, protein length 1374 bp, 458 aa
Immediate neighbours acoC, acoR
Sequences Protein DNA DNA_with_flanks
Genetic context
AcoL context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AcoL expression.png















Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

AcoR regulon, CcpA regulon, SigL regulon

The gene

Basic information

  • Locus tag: BSU08090

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Protein N(6)-(dihydrolipoyl)lysine + NAD+ = protein N(6)-(lipoyl)lysine + NADH (according to Swiss-Prot)
  • Protein family: class-I pyridine nucleotide-disulfide oxidoreductase family (according to Swiss-Prot)

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

  • Additional information:
    • the mRNA is very stable (half-life > 15 min) PubMed
    • the mRNA is substantially stabilized upon depletion of RNase Y PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 290 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 233 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 555 PubMed

Biological materials

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

Labs working on this gene/protein

Michel Debarbouille, Pasteur Institute, Paris, France Homepage

Your additional remarks

References

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)

Heike Reents, Richard Münch, Thorben Dammeyer, Dieter Jahn, Elisabeth Härtig
The Fnr regulon of Bacillus subtilis.
J Bacteriol: 2006, 188(3);1103-12
[PubMed:16428414] [WorldCat.org] [DOI] (P p)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [WorldCat.org] [DOI] (P p)

N O Ali, J Bignon, G Rapoport, M Debarbouille
Regulation of the acetoin catabolic pathway is controlled by sigma L in Bacillus subtilis.
J Bacteriol: 2001, 183(8);2497-504
[PubMed:11274109] [WorldCat.org] [DOI] (P p)

Y Miwa, A Nakata, A Ogiwara, M Yamamoto, Y Fujita
Evaluation and characterization of catabolite-responsive elements (cre) of Bacillus subtilis.
Nucleic Acids Res: 2000, 28(5);1206-10
[PubMed:10666464] [WorldCat.org] [DOI] (I p)

M Huang, F B Oppermann-Sanio, A Steinbüchel
Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway.
J Bacteriol: 1999, 181(12);3837-41
[PubMed:10368162] [WorldCat.org] [DOI] (P p)