Analysis of the transcriptional activity of the hut promoter in Bacillus subtilis and identification of a cis-acting regulatory region associated with catabolite repression downstream from the site of transcription

Mol Microbiol. 1992 Sep;6(18):2573-82. doi: 10.1111/j.1365-2958.1992.tb01434.x.

Abstract

Levels of transcripts initiated at a hut promoter in Bacillus subtilis were analysed. The addition of histidine to the culture medium increased the level of the transcript sixfold. In the presence of histidine and glucose together, the level of the transcript was reduced to the level in the absence of induction. Furthermore, addition of a mixture of 16 amino acids to cultures of induced cells and of catabolite-repressed cells decreased levels of the transcript 16-fold and 2.6-fold, respectively. Thus, it appears that at least three regulatory mechanisms associated with induction, catabolite repression, and amino acid repression, control the transcriptional activity of the hut promoter. Expression of the hut promoter-lacZ fusions that contained various regions of the hutP gene and deletion analysis of the hutP region revealed a cis-acting sequence associated with catabolite repression that was located between positions +204 and +231 or around position +203.

MeSH terms

  • Amino Acids / pharmacology
  • Bacillus subtilis / genetics*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Gene Expression Regulation, Bacterial* / drug effects
  • Genes, Bacterial*
  • Glucose / pharmacology
  • Histidine / metabolism*
  • Histidine / pharmacology
  • Histidine Ammonia-Lyase / genetics
  • Histidine Ammonia-Lyase / metabolism
  • Hydrolases / genetics
  • Hydrolases / metabolism
  • Molecular Sequence Data
  • Operon*
  • Promoter Regions, Genetic*
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / genetics
  • Regulatory Sequences, Nucleic Acid
  • Transcription, Genetic* / drug effects
  • Urocanate Hydratase / genetics
  • Urocanate Hydratase / metabolism

Substances

  • Amino Acids
  • Bacterial Proteins
  • Recombinant Fusion Proteins
  • Histidine
  • Hydrolases
  • EE57C protein, Bacillus subtilis
  • Urocanate Hydratase
  • Histidine Ammonia-Lyase
  • Glucose