Aromatic degradative pathways in Acinetobacter baylyi underlie carbon catabolite repression

Microbiology (Reading). 2008 Oct;154(Pt 10):3095-3103. doi: 10.1099/mic.0.2008/016907-0.


Carbon catabolite repression is an important mechanism allowing efficient carbon source utilization. In the soil bacterium Acinetobacter baylyi, this mechanism has been shown to apply to the aromatic degradative pathways for the substrates protocatechuate, p-hydroxybenzoate and vanillate. In this investigation, transcriptional fusions with the gene for luciferase in the gene clusters for the degradation of benzyl esters, anthranilate, benzoate, hydroxycinnamates and dicarboxylates (are, ant, ben, hca and dca genes) were constructed and established in the chromosome of A. baylyi. The respective strains revealed the presence of strong carbon catabolite repression at the transcriptional level. In all cases, succinate and acetate in combination had the strongest repressing effect, and pyruvate (or lactate in case of the ben and hca genes) allowed the highest expression when these carbon sources were supplied together with the respective inducer. The pattern of repression for the different cosubstrates was similar for all operons investigated and was also observed in the absence of the respective inducing compounds, indicating a mechanism that is independent of the respective specific regulators. Repression by acetate and succinate varied between 88 % for the hca genes and 99 % for the pca genes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetates / metabolism
  • Acinetobacter / genetics
  • Acinetobacter / metabolism*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Biodegradation, Environmental
  • Carbon / metabolism*
  • Chromosomes, Bacterial
  • DNA, Bacterial / genetics
  • Gene Expression Regulation, Bacterial*
  • Luciferases, Firefly
  • Operon*
  • Plasmids
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Succinic Acid / metabolism
  • Transcription, Genetic*
  • Transformation, Bacterial


  • Acetates
  • Bacterial Proteins
  • DNA, Bacterial
  • Recombinant Fusion Proteins
  • luciferase, Photinus
  • Carbon
  • Succinic Acid
  • Luciferases, Firefly